2a2b: Difference between revisions

Revision as of 00:29, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2a2b.png

Template:STRUCTURE 2a2b

Curvacin ACurvacin A

Template:ABSTRACT PUBMED 16331975

About this StructureAbout this Structure

2A2B is a Single protein structure of sequence from Lactobacillus curvatus. Full experimental 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

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OCA

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 {{STRUCTURE_2a2b|  PDB=2a2b  |  SCENE=  }}
-'''Curvacin A'''
+===Curvacin A===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16331975}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16331975 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16331975}}
 ==About this Structure==
-A2B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_curvatus Lactobacillus curvatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A2B OCA].
+A2B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_curvatus Lactobacillus curvatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A2B OCA].
 ==Reference==
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 [[Category: Beta-sheet like strukture]]
 [[Category: Peptide]]
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