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| [[Image:1ohn.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1ohn| PDB=1ohn | SCENE= }} | | {{STRUCTURE_1ohn| PDB=1ohn | SCENE= }} |
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| '''THREE-DIMENSIONAL STRUCTURE IN LIPID MICELLES OF THE PEDIOCIN-LIKE ANTIMICROBIAL PEPTIDE SAKACIN P.'''
| | ===THREE-DIMENSIONAL STRUCTURE IN LIPID MICELLES OF THE PEDIOCIN-LIKE ANTIMICROBIAL PEPTIDE SAKACIN P.=== |
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| ==Overview==
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| The three-dimensional structures in dodecylphosphocholine (DPC) micelles and in trifluoroethanol (TFE) of the pediocin-like antimicrobial peptide sakacin P and an engineered variant of sakacin P (termed sakP[N24C+44C]) have been determined by use of nuclear magnetic resonance spectroscopy. SakP[N24C+44C] has an inserted non-native activity- and structure-stabilizing C-terminal disulfide bridge that ties the C-terminus to the middle part of the peptide. In the presence of DPC, the cationic N-terminal region (residues 1-17) of both peptides has an S-shaped conformation that is reminiscent of a three-stranded antiparallel beta-sheet and that is more pronounced when the peptide was dissolved in TFE instead of DPC. The four positively charged residues located in the N-terminal part are found pointing to the same direction. For both peptides, the N-terminal region is followed by a well-defined central amphiphilic alpha-helix (residues 18-33), and this in turn is followed by the C-terminal tail (residues 34-43 for sakacin P and 34-44 for sakP[N24C+44C]) that lacks any apparent common secondary structural motif. In the presence of DPC, the C-terminal tails in both peptides fold back onto the central alpha-helix, thereby creating a hairpin-like structure in the C-terminal halves. The lack of long-range NOEs between the beta-sheet Nu-terminal region and the hairpin-like C-terminal half indicates that there is a flexible hinge between these regions. We discuss which implications such a structural arrangement has on the interaction with the target cell membrane. | | The line below this paragraph, {{ABSTRACT_PUBMED_14516192}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14516192 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14516192}} |
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| ==About this Structure== | | ==About this Structure== |
| 1OHN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_sakei Lactobacillus sakei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OHN OCA]. | | 1OHN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_sakei Lactobacillus sakei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OHN OCA]. |
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| ==Reference== | | ==Reference== |
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| [[Category: Pediocin-like bacteriocin]] | | [[Category: Pediocin-like bacteriocin]] |
| [[Category: Sakacin antibiotic]] | | [[Category: Sakacin antibiotic]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:51:35 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:46:36 2008'' |
