1o83: Difference between revisions
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[[ | ==CRYSTAL STRUCTURE OF BACTERIOCIN AS-48 AT PH 7.5, PHOSPHATE BOUND. CRYSTAL FORM I== | ||
<StructureSection load='1o83' size='340' side='right' caption='[[1o83]], [[Resolution|resolution]] 1.64Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1o83]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O83 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e68|1e68]], [[1o82|1o82]], [[1o84|1o84]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o83 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o83 RCSB], [http://www.ebi.ac.uk/pdbsum/1o83 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The bacteriocin AS-48 is a membrane-interacting peptide, which displays a broad anti-microbial spectrum against Gram-positive and Gram-negative bacteria. The NMR structure of AS-48 at pH 3 has been solved. The analysis of this structure suggests that the mechanism of AS-48 anti-bacterial activity involves the accumulation of positively charged molecules at the membrane surface leading to a disruption of the membrane potential. Here, we report the high-resolution crystal structure of AS-48 and sedimentation equilibrium experiments showing that this bacteriocin is able to adopt different oligomeric structures according to the physicochemical environment. The analysis of these structures suggests a mechanism for molecular function of AS-48 involving a transition from a water-soluble form to a membrane-bound state upon membrane binding. | |||
Structure of bacteriocin AS-48: from soluble state to membrane bound state.,Sanchez-Barrena MJ, Martinez-Ripoll M, Galvez A, Valdivia E, Maqueda M, Cruz V, Albert A J Mol Biol. 2003 Nov 28;334(3):541-9. PMID:14623193<ref>PMID:14623193</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Enterococcus faecalis]] | [[Category: Enterococcus faecalis]] | ||
[[Category: Albert, A.]] | [[Category: Albert, A.]] | ||
Revision as of 06:47, 9 June 2014
CRYSTAL STRUCTURE OF BACTERIOCIN AS-48 AT PH 7.5, PHOSPHATE BOUND. CRYSTAL FORM I
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