1og7
From Proteopedia
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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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[[Category: Nissen-Meyer, J.]] | [[Category: Nissen-Meyer, J.]] | ||
[[Category: Uteng, M.]] | [[Category: Uteng, M.]] | ||
| - | [[Category: | + | [[Category: Antibiotic]] |
| - | [[Category: | + | [[Category: Antimicrobial peptide]] |
| - | [[Category: | + | [[Category: Pediocin-like bacteriocin]] |
| - | [[Category: | + | [[Category: Sakacin p]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:48:28 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:48, 3 May 2008
THREE-DIMENSIONAL STRUCTURE IN LIPID MICELLES OF THE PEDIOCIN-LIKE ANTIMICROBIAL PEPTIDE SAKACIN P.
Overview
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.
About this Structure
1OG7 is a Single protein structure of sequence from Lactobacillus sakei. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P and a sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridge., Uteng M, Hauge HH, Markwick PR, Fimland G, Mantzilas D, Nissen-Meyer J, Muhle-Goll C, Biochemistry. 2003 Oct 7;42(39):11417-26. PMID:14516192 Page seeded by OCA on Sat May 3 03:48:28 2008
