2vat

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[[Image:2vat.png|left|200px]]
 
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{{STRUCTURE_2vat| PDB=2vat | SCENE= }}
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==Crystal structure of deacetylcephalosporin C acetyltransferase in complex with coenzyme A==
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<StructureSection load='2vat' size='340' side='right'caption='[[2vat]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2vat]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Acremonium_chrysogenum Acremonium chrysogenum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VAT 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]] 2.2&#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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2vat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vat OCA], [https://pdbe.org/2vat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vat RCSB], [https://www.ebi.ac.uk/pdbsum/2vat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vat ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CEFG_ACRCH CEFG_ACRCH] Catalyzes the conversion of deacetylcephalosporin C to cephalosporin C.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/va/2vat_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vat ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Deacetylcephalosporin C acetyltransferase (DAC-AT) catalyses the last step in the biosynthesis of cephalosporin C, a broad-spectrum beta-lactam antibiotic of large clinical importance. The acetyl transfer step has been suggested to be limiting for cephalosporin C biosynthesis, but has so far escaped detailed structural analysis. We present here the crystal structures of DAC-AT in complexes with reaction intermediates, providing crystallographic snapshots of the reaction mechanism. The enzyme is found to belong to the alpha/beta hydrolase class of acetyltransferases, and the structures support previous observations of a double displacement mechanism for the acetyl transfer reaction in other members of this class of enzymes. The structures of DAC-AT reported here provide evidence of a stable acyl-enzyme complex, thus underpinning a mechanism involving acetylation of a catalytic serine residue by acetyl coenzyme A, followed by transfer of the acetyl group to deacetylcephalosporin C through a suggested tetrahedral transition state.
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===CRYSTAL STRUCTURE OF DEACETYLCEPHALOSPORIN C ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A===
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The last step in cephalosporin C formation revealed: crystal structures of deacetylcephalosporin C acetyltransferase from Acremonium chrysogenum in complexes with reaction intermediates.,Lejon S, Ellis J, Valegard K J Mol Biol. 2008 Mar 28;377(3):935-44. Epub 2008 Jan 30. PMID:18279889<ref>PMID:18279889</ref>
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{{ABSTRACT_PUBMED_18279889}}
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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==About this Structure==
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<div class="pdbe-citations 2vat" style="background-color:#fffaf0;"></div>
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[[2vat]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Acremonium_chrysogenum Acremonium chrysogenum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VAT OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:018279889</ref><references group="xtra"/>
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</StructureSection>
[[Category: Acremonium chrysogenum]]
[[Category: Acremonium chrysogenum]]
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[[Category: Deacetylcephalosporin-C acetyltransferase]]
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[[Category: Large Structures]]
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[[Category: Ellis, J.]]
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[[Category: Ellis J]]
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[[Category: Lejon, S.]]
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[[Category: Lejon S]]
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[[Category: Valegard, K.]]
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[[Category: Valegard K]]
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[[Category: A/b- hydrolase fold]]
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[[Category: Acetyl coenzyme some]]
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[[Category: Acetyl transferase]]
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[[Category: Acyltransferase]]
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[[Category: Antibiotic biosynthesis]]
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[[Category: Cephalosporin biosynthesis]]
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[[Category: Transferase]]
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Current revision

Crystal structure of deacetylcephalosporin C acetyltransferase in complex with coenzyme A

PDB ID 2vat

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