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1o83

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[[Image:1o83.gif|left|200px]]<br />
 
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<applet load="1o83" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1o83, resolution 1.64&Aring;" />
 
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'''CRYSTAL STRUCTURE OF BACTERIOCIN AS-48 AT PH 7.5, PHOSPHATE BOUND. CRYSTAL FORM I'''<br />
 
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==Overview==
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==Crystal Structure of Bacteriocin AS-48 at pH 7.5, phosphate bound. Crystal form I==
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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.
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<StructureSection load='1o83' size='340' side='right'caption='[[1o83]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1o83]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1O83 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.64&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o83 OCA], [https://pdbe.org/1o83 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o83 RCSB], [https://www.ebi.ac.uk/pdbsum/1o83 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o83 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q47765_ENTFL Q47765_ENTFL]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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1O83 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis] with PO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O83 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14623193 14623193]
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</div>
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<div class="pdbe-citations 1o83" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Enterococcus faecalis]]
[[Category: Enterococcus faecalis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Albert, A.]]
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[[Category: Albert A]]
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[[Category: Cruz, V.]]
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[[Category: Cruz V]]
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[[Category: Galvez, A.]]
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[[Category: Galvez A]]
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[[Category: Maqueda, M.]]
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[[Category: Maqueda M]]
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[[Category: Martinez-Ripoll, M.]]
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[[Category: Martinez-Ripoll M]]
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[[Category: Sanchez-Barrena, M.J.]]
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[[Category: Sanchez-Barrena MJ]]
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[[Category: Valdivia, E.]]
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[[Category: Valdivia E]]
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[[Category: GOL]]
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[[Category: PO4]]
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[[Category: antibacterial peptide]]
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[[Category: bacteriocin]]
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[[Category: cyclic polypeptide]]
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[[Category: membrane permeabilization]]
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[[Category: protein crystallography]]
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[[Category: protein membrane interaction]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:00:02 2007''
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Current revision

Crystal Structure of Bacteriocin AS-48 at pH 7.5, phosphate bound. Crystal form I

PDB ID 1o83

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