2a2b
From Proteopedia
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Curvacin A
Overview
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.
About this Structure
2A2B is a Single protein structure of sequence from Lactobacillus curvatus. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide curvacin A., Haugen HS, Fimland G, Nissen-Meyer J, Kristiansen PE, Biochemistry. 2005 Dec 13;44(49):16149-57. PMID:16331975
Page seeded by OCA on Wed Nov 21 07:52:47 2007
