1o83
From Proteopedia
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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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Categories: Enterococcus faecalis | Albert, A. | Cruz, V. | Galvez, A. | Maqueda, M. | Martinez-Ripoll, M. | Sanchez-Barrena, M J. | Valdivia, E. | Antibacterial peptide | Bacteriocin | Cyclic polypeptide | Membrane permeabilization | Peptide antibiotic | Protein crystallography | Protein membrane interaction