2a2b: Difference between revisions
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==Curvacin A== | ==Curvacin A== | ||
<StructureSection load='2a2b' size='340' side='right' caption='[[2a2b]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2a2b' size='340' side='right' caption='[[2a2b]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2a2b]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A2B FirstGlance]. <br> | <table><tr><td colspan='2'>[[2a2b]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A2B FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2a2b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a2b RCSB], [http://www.ebi.ac.uk/pdbsum/2a2b PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2a2b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a2b RCSB], [http://www.ebi.ac.uk/pdbsum/2a2b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2a2b ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a2/2a2b_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a2/2a2b_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 10:05, 9 May 2018
Curvacin ACurvacin A
Structural highlights
Function[SAKA_LACCU] Bactericidal activity; inhibits closely related Lactobacilli, Listeria monocytogenes and ivanovvi, Enterococcus faecalis, Carnobacterium sp and Brocothrix thermosphacta. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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