Per Eugen Kristiansen

• Meuskens, Ina; Kristiansen, Per Eugen; Bardiaux, Benjamin; Koynarev, Vladimir Rosenov; Hatlem, Daniel & Prydz, Kristian [Show all 9 contributors for this article] (2023). A poly-proline II helix in YadA from Yersinia enterocolitica serotype O:9 facilitates heparin binding through electrostatic interactions. The FEBS Journal. ISSN 1742-464X. 291(4), p. 761–777. doi: 10.1111/febs.17001. Full text in Research Archive
• Hatlem, Daniel; Christensen, Mikkel; Broeker, Nina; Kristiansen, Per Eugen; Lund, Reidar & Barbirz, Stefanie [Show all 7 contributors for this article] (2023). A trimeric coiled-coil motif binds bacterial lipopolysaccharides with picomolar affinity. Frontiers in Cellular and Infection Microbiology. ISSN 2235-2988. 13. doi: 10.3389/fcimb.2023.1125482. Full text in Research Archive
• Andersen, Thorny Cesilie Bie; Kristiansen, Per Eugen; Huszenicza, Zsuzsa; Johansson, Maria U.; Gopalakrishnan, Ramakrishna Prabhu & Kjelstrup, Hanna [Show all 15 contributors for this article] (2019). The SH3 domains of the protein kinases ITK and LCK compete for adjacent sites on T cell-specific adapter protein. Journal of Biological Chemistry. ISSN 0021-9258. 294(42), p. 15480–15494. doi: 10.1074/jbc.RA119.008318. Full text in Research Archive
• Ekblad, Bie & Kristiansen, Per Eugen (2019). NMR structures and mutational analysis of the two peptides constituting the bacteriocin plantaricin S. Scientific Reports. ISSN 2045-2322. 9(1). doi: 10.1038/s41598-019-38518-6. Full text in Research Archive
• Ovchinnikov, Kirill; Kristiansen, Per Eugen; Straume, Daniel; Jensen, Marianne Slang; Aleksandrzak-Piekarczyk, Tamara & Nes, Ingolf [Show all 7 contributors for this article] (2017). The leaderless bacteriocin enterocin K1 is highly potent against Enterococcus faecium: A study on structure, target spectrum and receptor. Frontiers in Microbiology. ISSN 1664-302X. 8, p. 1–12. doi: 10.3389/fmicb.2017.00774. Full text in Research Archive
• Hatlem, Daniel; Heggelund, Julie Elisabeth; Burschowsky, Daniel; Krengel, Ute & Kristiansen, Per Eugen (2017). 1H, 13C, 15N backbone assignment of the human heat-labile enterotoxin B-pentamer and chemical shift mapping of neolactotetraose binding. Biomolecular NMR Assignments. ISSN 1874-2718. 11(1), p. 99–104. doi: 10.1007/s12104-017-9728-9. Full text in Research Archive
• Kristiansen, Per Eugen; Persson, Cecilia; Fuochi, Virginia; Pedersen, Anders; Karlsson, Göran & Nissen-Meyer, Jon [Show all 7 contributors for this article] (2016). Nuclear Magnetic Resonance Structure and Mutational Analysis of the Lactococcin A Immunity Protein. Biochemistry. ISSN 0006-2960. 55(45), p. 6250–6257. doi: 10.1021/acs.biochem.6b00848.
• Ekblad, Bie; Kyriakou, Panagiota K.; Oppegård, Camilla; Nissen-Meyer, Jon; Kaznessis, Yiannis N & Kristiansen, Per Eugen (2016). Structure-Function Analysis of the Two-Peptide Bacteriocin Plantaricin EF. Biochemistry. ISSN 0006-2960. 55(36), p. 5106–5116. doi: 10.1021/acs.biochem.6b00588.
• Kyriakou, Panagiota K.; Ekblad, Bie; Kristiansen, Per Eugen & Kaznessis, Yiannis N (2016). Interactions of a class IIb bacteriocin with a model lipid bilayer, investigated through molecular dynamics simulations. Biochimica et Biophysica Acta - Biomembranes. ISSN 0005-2736. 1858(4), p. 824–835. doi: 10.1016/j.bbamem.2016.01.005.
• Strömstedt, Adam A.; Kristiansen, Per Eugen; Gunasekera, Sunithi; Grob, Nathalie; Skjeldal, Lars & Göransson, Ulf (2016). Selective membrane disruption by the cyclotide kalata B7: complex ions and essential functional groups in the phosphatidylethanolamine binding pocket. Biochimica et Biophysica Acta - Biomembranes. ISSN 0005-2736. 1858(6), p. 1317–1327. doi: 10.1016/j.bbamem.2016.02.013.
• Rahman, Mohummad Aminur; Kristiansen, Per Eugen; Veiseth, Silje Veie; Andersen, Jan Terje; Yap, Kyoko L. & Zhou, Ming-Ming [Show all 9 contributors for this article] (2014). The arabidopsis histone methyltransferase SUVR4 binds ubiquitin via a domain with a four-helix bundle structure. Biochemistry. ISSN 0006-2960. 53(13), p. 2091–2100. doi: 10.1021/bi401436h.
• Ovchinnikov, Kirill V.; Kristiansen, Per Eugen; Uzelac, Gordana; Topisirovic, Ljubisa; Kojic, Milan & Nissen-Meyer, Jon [Show all 8 contributors for this article] (2014). Defining the Structure and Receptor Binding Domain of the Leaderless Bacteriocin LsbB. Journal of Biological Chemistry. ISSN 0021-9258. 289(34), p. 23838–23845. doi: 10.1074/jbc.M114.579698.
• Andersen, Thorny Cesilie Bie; Lindsjø, Kjersti; Hem, Cecilie Anne Dahl; Koll, Lise; Kristiansen, Per Eugen & Skjeldal, Lars [Show all 8 contributors for this article] (2014). Solubility of recombinant Src homology 2 domains expressed in E. coli can be predicted by TANGO. BMC Biotechnology. ISSN 1472-6750. 14(3). doi: 10.1186/1472-6750-14-3. Full text in Research Archive
• Zegeye, Ephrem Debebe; Balasingham, Seetha ; Lærdahl, Jon Kristen; Homberset, Håvard; Kristiansen, Per Eugen & Tønjum, Tone (2014). Effects of conserved residues and naturally occurring mutations on Mycobacterium tuberculosis RecG helicase activity. Microbiology (Reading). ISSN 1350-0872. 160(1), p. 217–227. doi: 10.1099/mic.0.072140-0. Show summary

  RecG is a helicase that is conserved in nearly all bacterial species. The prototypical Escherichia coli RecG promotes regression of stalled replication forks, participates in DNA recombination and DNA repair, and prevents aberrant replication. Mycobacterium tuberculosis RecG (RecGMtb) is a DNA-dependent ATPase that unwinds a variety of DNA substrates, although its preferred substrate is a Holliday junction. Here, we performed site-directed mutagenesis of selected residues in the wedge domain and motifs Q, I, Ib and VI of RecGMtb. Three of the 10 substitution mutations engineered were detected previously as naturally occurring SNPs in the gene encoding RecGMtb. Alanine substitution mutations at residues Q292, F286, K321 and R627 abolished the RecGMtb unwinding activity, whilst RecGMtb F99A, P285S and T408A mutants exhibited ~25-50 % lower unwinding activity than WT. We also found that RecGMtb bound ATP in the absence of a DNA cofactor.

• Myrset, Heidi; Fæste, Christiane Kruse; Kristiansen, Per Eugen & Dooper, Maaike (2013). Mapping of the Immunodominant Regions of Shrimp Tropomyosin Pan b 1 by Human IgE-Binding and IgE Receptor Crosslinking Studies. International Archives of Allergy and Immunology. ISSN 1018-2438. 162(1), p. 25–38. doi: 10.1159/000350791.
• Hoppmann, Verena; Thorstensen, Tage; Kristiansen, Per Eugen; Veiseth, Silje Veie; Rahman, Mohummad Aminur & Finne, Kenneth [Show all 8 contributors for this article] (2011). The CW domain, a new histone recognition module in chromatin proteins. EMBO Journal. ISSN 0261-4189. 30(10), p. 1939–1952. doi: 10.1038/emboj.2011.108.
• Tadesse, Margey; Tabudravu, Jioji N.; Jaspars, Marcel; Strøm, Morten B.; Hansen, Espen & Andersen, Jeanette hammer [Show all 8 contributors for this article] (2011). The antibacterial ent-Eusynstyelamide B and Eusynstyelamides D, E and F from the Arctic Bryozoan Tegella cf. spitzbergensis. Journal of natural products. ISSN 0163-3864. 74, p. 837–841. doi: 10.1021/np100499c. Show summary

  The brominated tryptophan-derived ent-eusynstyelamide B (1) and three new derivatives, eusynstyelamides D, E, and F (2-4), were isolated from the Arctic bryozoan Tegella cf. spitzbergensis. The structures were elucidated by spectroscopic methods including 1D and 2D NMR and analysis of mass spectrometric data. The enantiomer of 1, eusynstyelamide B, has previously been isolated from the Australian ascidian Eusynstyela latericius. Antimicrobial activities are here reported for 1-4, with minimum inhibitory concentrations (MIC) as low as 6.25 μg/mL for 1 and 4 against Staphylococcus aureus. Eusynstyelamides 2 and 3 showed weak cytotoxic activity against the human melanoma A 2058 cell line

• Tadesse, Margey; Svenson, Johan ; Jaspars, Marcel; Strøm, Morten B.; Abdelrahman, Mostafa H. & Andersen, Jeanette hammer [Show all 10 contributors for this article] (2011). Synoxazolidinone C; a bicyclic member of the synoxazolidinone family with antibacterial and anticancer activities. Tetrahedron Letters. ISSN 0040-4039. 52, p. 1804–1806. doi: 10.1016/j.tetlet.2011.02.027. Show summary

  Synoxazolidinone C is a new member of the synoxazolidinone family of compounds which are dibrominated guanidinium 4-oxazolidinones isolated from the sub-Arctic ascidian Synoicum pulmonaria. The compound was isolated along with synoxazolidinones A and B from the same ascidian extract. Spectroscopic methods revealed that the synoxazolidinone C differed from the other synoxazolidinones by an unprecedented bicyclic partial structure, containing an additional pyrrolidine ring. Synoxazolidinone C exhibited both antibacterial and anticancer activities.

• Nissen-Meyer, Jon; Oppegård, Camilla; Rogne, Per Anders; Haugen, Helen Sophie & Kristiansen, Per Eugen (2010). Structure and mode-of-action of the two-peptide (class-IIb) bacteriocins. Probiotics and Antimicrobial Proteins. ISSN 1867-1306. 2, p. 52–60. doi: 10.1007/s12602-009-9021-z.
• Oppegård, Camilla; Rogne, Per Anders; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2010). Structure analysis of the two-peptide bacteriocin lactococcin G by introducing D-amino acid residues. Microbiology (Reading). ISSN 1350-0872. 156, p. 1883–1889. doi: 10.1099/mic.0.038430-0.
• Gunnarsen, Kristin Støen; Lunde, Elin; Kristiansen, Per Eugen; Bogen, Bjarne; Sandlie, Inger & Løset, Geir Åge (2010). Periplasmic expression of soluble single chain T cell receptors is rescued by the chaperone FkpA. BMC Biotechnology. ISSN 1472-6750. 10. doi: 10.1186/1472-6750-10-8. Full text in Research Archive
• Nissen-Meyer, Jon; Rogne, Per Anders; Oppegård, Camilla; Haugen, Helen Sophie & Kristiansen, Per Eugen (2009). Structure-function relationships of the non-lanthionine-containing peptide (class II) bacteriocin produced by gram-positive bacteria. Current Pharmaceutical Biotechnology. ISSN 1389-2010. 10(1), p. 19–37.
• Berntzen, Gøril; Andersen, Jan Terje; Ustgård, Kristine; Ustgård, Kristine; Michaelsen, Terje Einar & Mousavi, Darbi Seyed Ali [Show all 13 contributors for this article] (2009). Identification of a High Affinity Fc gamma RIIA-binding Peptide That Distinguishes Fc gamma RIIA from Fc gamma RIIB and Exploits Fc gamma RIIA-mediated Phagocytosis and Degradation. Journal of Biological Chemistry. ISSN 0021-9258. 284(2), p. 1126–1135. doi: 10.1074/jbc.M803584200. Full text in Research Archive
• Rogne, Per Anders; Haugen, Mads Christofer; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2009). Three-dimensional structure of the two-peptide bacteriocin plantaricin JK. Peptides. ISSN 0196-9781. 30(9), p. 1613–1621. doi: 10.1016/j.peptides.2009.06.010. Show summary

  The three-dimensional structures of the two peptides, PlnJ and PlnK, that constitutes the two-peptide bacteriocin plantaricin JK have been solved in water/TFE and water/DPC-micellar solutions using nuclear magnetic resonance (NMR) spectroscopy. PlnJ, a 25 residue peptide, has an N-terminal amphiphilic α-helix between Trp-3 and Tyr-15. The 32 residues long PlnK forms a central amphiphilic α-helix between Gly-9 and Leu-24. Measurements of the effect on anti-microbial activity of single glycine replacements in PlnJ and PlnK show that Gly-13 and Gly-17 in both peptides are very sensitive, giving more than a 100-fold reduction in activity when large residues replace glycine. In variants where other glycine residues, Gly-20 in PlnJ and Gly-7, Gly-9, Gly-24 and Gly-25 in PlnK, were replaced, the activity was reduced less than 10-fold. It is proposed that the detrimental effect on activity when exchanging Gly-13 and Gly-17 in PlnJ and PlnK is a result of reduced ability of the two peptides to interact through the GxxxG-motifs constituting Gly-13 and Gly-17.

• Fimland, N; Rogne, Per Anders; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2008). Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin plantaricin EF. Biochimica et Biophysica Acta - Proteins and Proteomics. ISSN 1570-9639. 1784(11), p. 1711–1719. doi: 10.1016/j.bbapap.2008.05.003.
• Haugen, Helen Sophie; Kristiansen, Per Eugen; Fimland, Gunnar & Nissen-Meyer, Jon (2008). Mutational Analysis of the Class IIa Bacteriocin Curvacin A and Its Orientation in Target Cell Membranes. Applied and Environmental Microbiology. ISSN 0099-2240. 74(21), p. 6766–6773. doi: 10.1128/AEM.01068-08.
• Oppegård, Camilla; Schmidt, Juliane; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2008). Mutational analysis of putative helix-helix interacting GxxxG-Motifs and tryptophan residues in the two-peptide bacteriocin lactococcin G. Biochemistry. ISSN 0006-2960. 47, p. 5242–5249. doi: 10.1021/bi800289w.
• Rogne, Per Anders; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2008). Three-dimensional structure of the two peptides that constitute the two-peptide bacteriocin lactococcin G. Biochimica et Biophysica Acta - Proteins and Proteomics. ISSN 1570-9639. 1784. doi: 10.1016/j.bbapap.2007.12.002.
• Oppegård, Camilla; Rogne, Per Anders; Emanuelsen, Linda; Kristiansen, Per Eugen; Fimland, Gunnar & Nissen-Meyer, Jon (2007). The Two-Peptide Class II Bacteriocins: Structure, Production, and Mode of Action. Journal of Molecular Microbiology and Biotechnology. ISSN 1464-1801. 13, p. 210–219. doi: 10.1159/000104750.
• Johnsborg, Ola; Kristiansen, Per Eugen; Blomqvist, Trinelise & Håvarstein, Leiv Sigve (2006). A hydrophobic patch in the competence-stimulating peptide, a pneumococcal competence pheromone, is essential for specificity and biological activity. Journal of Bacteriology. ISSN 0021-9193. 188(5), p. 1744–1749. Show summary

  Induction competence for natural genetic transformation in Streptococcus pneumoniae depends on pheromone-mediated cell-cell communication and a signaling pathway consisting of the competence-stimulating peptide (CSP), its membrane-embedded histidine kinase receptor ComD, and the cognate response regulator ComE. Extensive screening of pneumococcal isolates has revealed that two major CSP variants, CSP1 and CSP2, are found in members of this species. Even though the primary structures of CSP1 and CSP2 are about 50% identical, they are highly specific for their respective receptors, ComD1 and ComD2. In the present work, we have investigated the structural basis of this specificity by determining the three-dimensional structure of CSP1 from nuclear magnetic resonance data and comparing the agonist activity of a number of CSP1/CSP2 hybrid peptides toward the ComD1 and ComD2 receptors. Our results show that upon exposure to membrane-mimicking environments, the 17-amino-acid CSP1 pheromone adopts an amphiphilic alpha-helical configuration stretching from residue 6 to residue 12. Furthermore, the pattern of agonist activity displayed by the various hybrid peptides revealed that hydrophobic amino acids, some of which are situated on the nonpolar side of the alpha-helix, strongly contribute to CSP specificity. Together, these data indicate that the identified alpha-helix is an important structural feature of CSP1 which is essential for effective receptor recognition under natural conditions.

• Kristiansen, Per Eugen; Carravetta, Marina; Van Beek, Jacco D; Levitt, Malcolm H & Lai, Wau Cheu (2006). Theory and applications of supercycled symmetry-based recoupling sequences in solid-state nuclear magnetic resonance. Journal of Chemical Physics. ISSN 0021-9606. 123(23).
• Johnsborg, Ola; Kristiansen, Per Eugen; Blomquist, T & Havarstein, LS (2006). A hydrophobic patch in the competence-stimulating peptide, a pneumococcal competence pheromone, is essential for specificity and biological activity. Journal of Bacteriology. ISSN 0021-9193. 188(5), p. 1744–1749.
• Fimland, Gunnar; Pirneskoski, J; Kaewsrichan, J; Jutila, A; Kristiansen, Per Eugen & Kinnunen, P K [Show all 7 contributors for this article] (2006). Mutational analysis and membrane-interactions of the beta-sheet-like N-terminal domain of the pediocin-like antimicrobial peptide sakacin P. Biochimica et Biophysica Acta - Proteins and Proteomics. ISSN 1570-9639. 1764(6), p. 1132–1140.
• Kristiansen, Per Eugen; Fimland, Gunnar; Mantzilas, Dimitrios & Nissen-Meyer, Jon (2005). Structure and mode of action of the membrane-permeabilizing antimicrobial peptide pheromone plantaricin A. Journal of Biological Chemistry. ISSN 0021-9258. 280, p. 22945–22950.
• Brouwer, DH; Kristiansen, Per Eugen; Fyfe, CA & Levitt, MH (2005). Symmetry-based Si-29 dipolar recoupling magic angle spinning NMR spectroscopy: A new method for investigating three-dimensional structures of zeolite frameworks. Journal of the American Chemical Society. ISSN 0002-7863. 127.
• Haugen, Helen Sophie; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2005). Three-Dimensional Structure in Lipid Micelles of the Pediocin-like Antimicrobial Peptide Curvacin A. Biochemistry. ISSN 0006-2960. 44(49), p. 16149–16157 . doi: 10.1021/bi051215u. Show summary

  The 3D structure of the membrane-permeabilizing 41-mer pediocin-like antimicrobial peptide curvacin A produced by lactic acid bacteria has been studied by NMR spectroscopy. In DPC micelles, the cationic and hydrophilic N-terminal half of the peptide forms an S-shaped beta-sheet-like domain stabilized by a disulfide bridge and a few hydrogen bonds. This domain is followed by two alpha-helices: a hydrophilic 6-mer helix between residues 19 and 24 and an amphiphilic/hydrophobic 11-mer helix between residues 29 and 39. There are two hinges in the peptide, one at residues 16-18 between the N-terminal S-shaped beta-sheet-like structure and the central 6-mer helix and one at residues 26-28 between the central helix and the 11-mer C-terminal helix. The latter helix is the only amphiphilic/hydrophobic part of the peptide and is thus presumably the part that penetrates into the hydrophobic phase of target-cell membranes. The hinge between the two helices may introduce the flexibility that allows the helix to dip into membranes. The helix-hinge-helix structure in the C-terminal half of curvacin A clearly distinguishes this peptide from the other pediocin-like peptides whose structures have been analyzed and suggests that curvacin A along with the structural homologues enterocin P and carnobacteriocin BM1 belong to a subgroup of the pediocin-like family of antimicrobial peptides.

• Kristiansen, Per Eugen; Carravetta, M; Lai, WC & Levitt, MH (2004). A robust pulse sequence for the determination of small homonuclear dipolar couplings in magic-angle spinning NMR. Chemical Physics Letters. ISSN 0009-2614. 390, p. 1–7.
• Kristiansen, Per Eugen; Hansen, Eddy Walther & Pedersen, Bjørn (2000). Phase distribution in polyethylene versus temperature probed by solid-state proton NMR free induction decay. Polymer. ISSN 0032-3861. 41, p. 311–321.
• Kristiansen, Per Eugen; Hansen, Eddy Walther & Pedersen, Bjørn (1999). Phase distribution during isothermal crystallization of polyethylene probed by solid-state proton NMR free induction decay. Journal of Physical Chemistry. ISSN 0022-3654. 103, p. 3552–3558.
• Hansen, Eddy Walther; Kristiansen, Per Eugen & Pedersen, Bjørn (1998). Chrystallinity of Polyethylene derived from solid-state proton NMR free induction decay. Journal of Physical Chemistry B. ISSN 1520-6106. 102, p. 5444–5450.

View all works in Cristin

• Meuskens, Ina; Kristiansen, Per Eugen; Bardiaux, Benjamin; Koynarev, Vladimir Rosenov; Hatlem, Daniel & Prydz, Kristian [Show all 9 contributors for this article] (2023). Strain variations in a bacterial adhesin lead to different binding partners in the pathogen Yersinia enterocolitica .
• Ovchinnikov, Kirill; Kristiansen, Per Eugen; Nes, Ingolf & Diep, Dzung Bao (2016). Structure-function and receptor study of LsbB family leaderless bacteriocins.
• Skjeldal, Lars & Kristiansen, Per Eugen (2015). NMR structure of kalata B7 ser mutant. Show summary

  PDB 2MWO

• Hatlem, Daniel; Heggelund, Julie Elisabeth; Burschowsky, Daniel; Kristiansen, Per Eugen & Krengel, Ute (2014). Characterization of Lipopolysaccharide Binding to the E.coli Heat-labile Enterotoxin.
• Myrset, Heidi; Faeste, C.K.; Kristiansen, Per Eugen; Egaas, Eliann & Dooper, Maaike (2013). Mapping of the immunodominant regions of shrimp tropomyosin Pan b 1 by basophil activation test and skin prick test. Allergy. European Journal of Allergy and Clinical Immunology. ISSN 0105-4538. 68, p. 34–34.
• Hatlem, Daniel; Heggelund, Julie Elisabeth; Burschowsky, Daniel; Kristiansen, Per Eugen & Krengel, Ute (2013). Characterization of Lipopolysaccharide binding to E.coli Heat-labile Enterotoxin.
• Ekblad, Bie; Jørgenrud, Benedicte Marie; Kristiansen, Per Eugen; Nissen-Meyer, Jon & Oppegård, Camilla (2013). Structure-Function Analysis of the Two-Peptide Bacteriocin Plantaricin EF by the use of NMR and In Vitro Site-Directed Mutagenesis.
• Tadesse, Margey; Strøm, Morten B.; Svenson, Johan ; Jaspars, Marcel; Milne, Bruce F. & Tabudravu, Jioji N. [Show all 13 contributors for this article] (2011). Antimicrobial compounds from cold-water marine organisms.
• Tadesse, Margey; Strøm, Morten B.; Svenson, Johan ; Jaspars, Marcel; Milne, Bruce F. & Tabudravu, Jioji N. [Show all 13 contributors for this article] (2011). Antimicrobial compounds from cold-water marine organisms.
• Tadesse, Margey; Strøm, Morten B.; Svenson, Johan ; Jaspars, Marcel; Milne, Bruce F. & Tabudravu, Jioji N. [Show all 13 contributors for this article] (2011). Antimicrobial compounds from cold-water marine organisms.
• Tadesse, Margey; Svenson, Johan; Jaspars, Marcel; Strøm, Morten B.; Abdelrahman, Mostafa H. & Andersen, Jeanette hammer [Show all 10 contributors for this article] (2011). Synoxazolidinone C; A bicyclic member of the synoxazolidinone family with antibacterial and anticancer activities. ChemInform. ISSN 0931-7597. 42(29). doi: 10.1002/chin.201129197.
• Oppegård, Camilla; Rogne, Per Anders; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2010). Structure-analysis of the two-peptide bacteriocin lactococcin G by introducing D-amino acid residues.
• Oppegård, Camilla; Rogne, Per Anders; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2009). Structure-analysis of the two-peptide bacteriocin lactococcin G by introducing D-amino acid residues.
• Oppegård, Camilla; Rogne, Per Anders; Schmidt, Juliane; Kristiansen, Per Eugen; Emanuelsen, Linda & Nissen-Meyer, Jon (2008). Structural and Functional Model of the Membrane-Permeabilizing Two-Peptide Bacteriocin Lactococcin G and its Cognate Immunity Protein.
• Oppegård, Camilla; Rogne, Per Anders; Schmidt, Juliane; Kristiansen, Per Eugen; Emanuelsen, Linda & Nissen-Meyer, Jon (2008). Structural and Functional Model of the Membrane-Permeabilizing Two-Peptide Bacteriocin Lactococcin G and its Cognate Immunity Protein.
• Oppegård, Camilla; Schmidt, Juliane; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2008). Analysis of the GxxxG motifs in the two-peptide bacteriocin lactococcin G by use of site-directed mutagenesis. Show summary

  Peptide bacteriocins kill bacteria by permeabilizing their membrane. Some peptide bacteriocins (referred to as two-peptide bacteriocins), such as lactococcin G, consist of two different peptides and both peptides must be present in order for the bacteriocin to kill the target bacteria. Circular dichroism (CD) studies indicate that the two peptides of two-peptide bacteriocins interact physically with each other and that they adopt an α-helical structure upon contact with target membranes. All two-peptide bacteriocins contain GxxxG-motifs which are known to mediate helix-helix interactions in membrane proteins. Many of the GxxxG-motifs in two-peptide bacteriocins are located in putative amphiphilic α-helical regions and may play an important role in peptide-peptide interactions. Lactococcin G contains three such GxxxG-motifs, two in the α-peptide (G7xxxG11 and G18xxxG22) and one in the β-peptide (G18xxxG22). In this study, site-directed mutagenesis combined with CD measurements were used to analyse the role of the three GxxxG-motifs. The results indicate that the G7xxxG11-motif in the α-peptide and G18xxxG22-motif in the β-peptide are important in helix-helix interactions between the two lactococcin G peptides and that the two peptides form a transmembrane helix-helix structure.

• Rogne, Per Anders; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2008). The Three-Dimensional Structure of the Two-Peptide Bacteriocin Lactococcin G.
• Haugen, Helen Sophie; Fimland, Gunnar; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2008). Structure and Position in Membranes of the Bacteriocin Curvacin A Based on NMR-structure and Mutagenesis Studies. Show summary

  Curvacin A is a pediocin-like (class IIa) bacteriocin produced by Lactabacillus curvatus LTH 1174. The three-dimensional structure of curvacin A has been determined by NMR-spectroscopy. The structure reveals that curvacin A consists of two structural elements: a cationic -sheet like N-terminal half followed by a helix-hinge-helix motif. The helix-hinge-helix motif is made up of a short polar helix and a longer C-terminal hydrophobic helix separated by a hinge region. Site-directed in vitro mutagenesis has been carried out on curvacin A. Based on these results along with the NMR-structure, a model for insertion of curvacin A in target membranes has been proposed. In this model, the N-terminal -sheet like half and the short central polar helix are positioned in the membrane interface, whereas the longer hydrophobic C-terminal helix penetrates into the hydrophobic core of membranes. Three glycine residues in the C-terminal helix form a GxxxG-like motif that might mediate close contact with an interaction partner allowing helix-helix interactions.

• Haugen, Helen Sophie; Fimland, Gunnar; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2008). Structure and Position in Membranes of the Bacteriocin Curvacin A Based on NMR-structure and Mutagenesis Studies. Show summary

  Lactic acid bacteria (LAB) produce antimicrobial peptides, generally termed bacteriocins. The bacteriocins are part of the innate defence system of the producing bacteria. Targeting the membrane of cells, the bacteriocins render the membrane permeable to ions and small molecules, thereby killing the cell. Curvacin A is a pediocin-like (class IIa) bacteriocin produced by Lactabacillus curvatus LTH 1174 (LMGT 2355). The three-dimensional structure of curvacin A has been determined by NMR-spectroscopy. The structure reveals that curvacin A consists of two structural elements: a cationic -sheet like N-terminal half followed by a helix-hinge-helix motif. The helix-hinge-helix motif is made up of a short polar helix and a longer C-terminal hydrophobic helix separated by a hinge region. Site-directed in vitro mutagenesis has been carried out on curvacin A. Based on these results along with the NMR-structure, a model for insertion of curvacin A in target membranes has been proposed. In this model, the N-terminal -sheet like half and the short central polar helix are positioned in the membrane interface, whereas the longer hydrophobic C-terminal helix penetrates into the hydrophobic core of membranes. Three glycine residues in the C-terminal helix form a GxxxG-like motif that might mediate close contact with an interaction partner allowing helix-helix interactions.

• Rogne, Per Anders; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2007). NMR-analysis of the 3-D structure of the two-peptide bacteriocin Lactococcin G. Show summary

  Lactococcin G is an unmodified two peptide bacteriocin. The bacteriocin consists of the 39 amino acid -peptide (LcnGα) and the 35 amino acid -peptide (LcnG). Both peptides,  and , are required in about equal amounts in order for the bacteriocin to permeabilize target-cell membranes and thereby exert its antimicrobial activity (Nissen-Meyer et al). The peptides are unstructured in water but becomes structured when in contact with membranes (Hauge et al). The three dimensional structure of the two peptides have been determined in a membrane mimicking environment using NMR (figure 1). The structures of the two peptides are α-helical and contains helix-helix interaction motifs.

• Rise, Frode; Krengel, Ute; Gørbitz, Carl Henrik; Nissen-Meyer, Jon; Kristiansen, Per Eugen & Davies, William (2007). THE UNIVERSITY OF OSLO BIOMOLECULAR STRUCTURE PLATFORM. Show summary

  In-depth understanding of the mode of action of proteins and other biomolecules relies to a large extent on knowledge of their three-dimensional structures. Such knowledge is necessary for understanding bio-recognition and response processes, and is required for rational design of specific pharmacological reagents. Consequently it is essential for research in the molecular biosciences to determine the structures of biomolecules. We have applied for funding. with a grant proposal to EMBIO, to establish and manage a “Biomolecular Structure Platform” at the University of Oslo. The intention of the platform is to make methods for structure determination of biomolecules available to a larger group of the biomedical and biological communities. Moreover, it is also aimed to provide assistance in large-scale production and purification of proteins for structural studies. The principle objectives and purposes of the “Biomolecular Structure-Platform” are to: 1. Establish and develop methods for large-scale production and purification of isotope labeled proteins and peptides for structural analysis. 2. Determine the structure of proteins under investigation by the contributing groups, and thereby gain detailed insight into how these proteins function at a molecular level. 3. Serve other research groups that need assistance in production and purification of 13C, 15N and Se-Met labeled proteins and peptides. 4. Provide assistance to other research groups that wish to analyze the structure of proteins, peptides and other biomolecules by NMR-spectroscopy and X-ray crystallography, mainly in the context of collaborative research. 5. Strengthen the expertise in both three-dimensional structure- and function- analysis of biological macromolecules by performing a variety of experiments and employing different structure determination tools and also by educating Ph.D.- and Master- degree students in structure determination and analysis. 6. Strengthen the expertise in large-scale production and purification of proteins by educating Ph.D.- and Master- degree students in relevant techniques.

• Kristiansen, Per Eugen; Sand, Sverre; Haug, Trude M; Sand, Olav; Fimland, Gunnar & Zhao, Hongxia [Show all 10 contributors for this article] (2006). Structure and Mode of Action of the Membrane-Permeabilizing Antimicrobial Peptide Pheromone Plantaricin A.
• Fimland, Gunnar; Johnsen, Line; Dalhus, Bjørn; Haugen, Helen Sofie; Kristiansen, Per Eugen & Nissen-Meyer, Jon (2006). Analysing the mode of action of pediocin-like bacteriocins and their immunity proteins by determining their NMR- and crystal-structures, and by genetic modifications.
• Rogne, Per Anders; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2006). NMR-analysis of the 3-D structure of the two-peptide bacteriocin lactococcin G. Show summary

  Lactococcin G is a bacteriocin that consists of two peptides, the  peptide with 39 residues and the peptide with 35 residues. Both peptides are required in about equal amounts in order for the bacteriocin to permeabilize target-cell membranes and thereby exert its antimicrobial activity. As determined by CD-spectroscopy, the two peptides interact with each other and become structured – adopting a partial amphiphilic -helical conformation – when exposed to membrane-like entities.[1] In this study, NMR-spectroscopy has been used to analyse the 3-D structure of the lactococcin G peptides seperatly upon exposure to dodecylphosphocoline micelles. The interactions between the two peptides will be the scope of further investigation. 15N labelled peptides were obtained using a fusion protein based over-expression system in E. coli. The peptides were assigned using 15N-HSQC-TOCSY and 15N-HSQC-NOESY in combination with 2D-TOCSY and NOESY spectra. The structures were calculated using both NOE-distance restraints and dihedral-angle restraints calculated on the basis of the chemical shift values [2] , using CYANA [3].

• Rogne, Per Anders; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2006). NMR-analysis of the 3-D structure of the two-peptide bacteriocin Lactococcin G. Show summary

  Lactococcin G is an unmodified two peptide bacteriocin, the name bacteriocin stems from its potential to kill bacteria. The bacteriocin consists of the 39 amino acid -peptide (LcnGα) and the 35 amino acid -peptide (LcnG) (figure 2). Both peptides,  and , are required in about equal amounts in order for the bacteriocin to permeabilize target-cell membranes and thereby exert its antimicrobial activity (Nissen-Meyer et al). The peptides are unstructured in water but becomes structured when in contact with membranes (Hauge et al). In this project, the three dimensional structure of the two peptides will be determined in a membrane mimicking environment using NMR.

• Rogne, Per Anders; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2006). NMR-analysis of the 3-D structure of the two-peptide bacteriocin Lactococcin G. Show summary

  Lactococcin G is an unmodified two peptide bacteriocin. The bacteriocin consists of the 39 amino acid -peptide (LcnGα) and the 35 amino acid -peptide (LcnG) (figure 4). Both peptides,  and , are required in about equal amounts in order for the bacteriocin to permeabilize target-cell membranes and thereby exert its antimicrobial activity (Nissen-Meyer et al). The peptides are unstructured in water but becomes structured when in contact with membranes (Hauge et al). In this project, the three dimensional structure of the two peptides will be determined in a membrane mimicking environment using NMR.

• Haugen, Helen Sofie; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2006). The three-dimensional NMR structure of th epediocin-like bacteriocin (antimicrobial peptide) curvacin A.
• Haugen, Helen Sofie; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2006). The three-dimensional NMR structure of the pediocin-like bacteriocin (antimicrobial peptide) curvacin A.
• Haugen, Helen Sofie; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2006). The three-dimensional NMR structure of the pediocin-like bacteriocin (antimicrobial peptide) curvacin A.
• Haugen, Helen Sofie; Fimland, Gunnar; Nissen-Meyer, Jon & Kristiansen, Per Eugen (2006). The three-dimensional NMR structure of th epediocin-like bacteriocin (antimicrobial peptide) curvacin A.
• Kristiansen, Per Eugen; Fimland, Gunnar & Nissen-Meyer, Jon (2006). The NMR structure and mode of action of the membrane-permeabilizing antimicrobial peptide pheromone plantaricin A.
• Kristiansen, Per Eugen; Fimland, Gunnar & Nissen-Meyer, Jon (2005). Structure and mode of action of the membrane permeabilizing antimicrobial peptide pheromone plantaricin A.
• Kristiansen, Per Eugen (2004). Application of Solid-state NMR Techniques to Probe Inter-atomic Distances in Solid.
• Kristiansen, Per Eugen; Nissen-Meyer, Jon & Fimland, Gunnar (2004). Mode of action of antimicrobial sakacin P peptides with biological membranes studied by calorimetry, circular dichroism and biological MAS NMR.
• Haugen, Helen sofie; Kristiansen, Per Eugen; Fimland, Gunnar & Nissen-Meyer, Jon (2004). Optimising the coditions for NMR structural analysis of the antimicrobial peptide curvacin A, a bacteriocin produced by Lactobacillus curvatus.
• Kristiansen, Per Eugen; Nissen-Meyer, Jon; Fimland, Gunnar & Haugen, Helen Sofie (2004). Optimizing the conditions for NMR structural analysis of the antimicrobial peptide Curvacin A, A bactericine produced by Lactobacillus Curvatus.
• Kristiansen, Per Eugen (2004). Mode of Action of Antimicrobial: Sakacin P Peptides with Biological Membranes Studied by Calorimetry, Circular Dichroism and Biological MAS NMR.

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