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1o84
From Proteopedia
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| - | [[ | + | ==CRYSTAL STRUCTURE OF BACTERIOCIN AS-48. N-DECYL-BETA-D-MALTOSIDE BOUND.== |
| + | <StructureSection load='1o84' size='340' side='right' caption='[[1o84]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1o84]] is a 2 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=1O84 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O84 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e68|1e68]], [[1o82|1o82]], [[1o83|1o83]]</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=1o84 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o84 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o84 RCSB], [http://www.ebi.ac.uk/pdbsum/1o84 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 18:43, 28 September 2014
CRYSTAL STRUCTURE OF BACTERIOCIN AS-48. N-DECYL-BETA-D-MALTOSIDE BOUND.
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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
