2a2b: Difference between revisions

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[[Image:2a2b.gif|left|200px]]
[[Image:2a2b.gif|left|200px]]


{{Structure
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{{STRUCTURE_2a2b| PDB=2a2b  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a2b OCA], [http://www.ebi.ac.uk/pdbsum/2a2b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2a2b RCSB]</span>
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'''Curvacin A'''
'''Curvacin A'''
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[[Category: Haugen, H S.]]
[[Category: Haugen, H S.]]
[[Category: Kristiansen, P E.]]
[[Category: Kristiansen, P E.]]
[[Category: alfa helix]]
[[Category: Alfa helix]]
[[Category: beta-sheet like strukture]]
[[Category: Beta-sheet like strukture]]
[[Category: peptide]]
[[Category: Peptide]]
 
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Revision as of 18:30, 3 May 2008

File:2a2b.gif

Template:STRUCTURE 2a2b

Curvacin A


OverviewOverview

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 StructureAbout this Structure

2A2B is a Single protein structure of sequence from Lactobacillus curvatus. Full crystallographic information is available from OCA.

ReferenceReference

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 Sat May 3 18:30:49 2008

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