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2vav
From Proteopedia
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| - | [[Image:2vav.png|left|200px]] | ||
| - | + | ==Crystal structure of deacetylcephalosporin C acetyltransferase (DAC-Soak)== | |
| + | <StructureSection load='2vav' size='340' side='right'caption='[[2vav]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2vav]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Acrch Acrch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VAV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VAV FirstGlance]. <br> | ||
| + | </td></tr><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=CSC:4-(3-ACETOXYMETHYL-2-CARBOXY-8-OXO-5-THIA-1-AZA-BICYCLO[4.2.0]OCT-2-EN-7-YLCARBAMOYL)-1-CARBOXY-BUTYL-AMMONIUM'>CSC</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OAS:O-ACETYLSERINE'>OAS</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vat|2vat]], [[2vax|2vax]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Deacetylcephalosporin-C_acetyltransferase Deacetylcephalosporin-C acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.175 2.3.1.175] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2vav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vav OCA], [http://pdbe.org/2vav PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vav RCSB], [http://www.ebi.ac.uk/pdbsum/2vav PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vav ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CEFG_ACRCH CEFG_ACRCH]] Catalyzes the conversion of deacetylcephalosporin C to cephalosporin C. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/va/2vav_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=2vav ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2vav" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | < | + | </StructureSection> |
| - | [[Category: | + | [[Category: Acrch]] |
[[Category: Deacetylcephalosporin-C acetyltransferase]] | [[Category: Deacetylcephalosporin-C acetyltransferase]] | ||
| - | [[Category: Ellis, J | + | [[Category: Large Structures]] |
| - | [[Category: Lejon, S | + | [[Category: Ellis, J]] |
| - | [[Category: Valegard, K | + | [[Category: Lejon, S]] |
| + | [[Category: Valegard, K]] | ||
[[Category: A/b- hydrolase fold]] | [[Category: A/b- hydrolase fold]] | ||
[[Category: Acetyl coenzyme some]] | [[Category: Acetyl coenzyme some]] | ||
Current revision
Crystal structure of deacetylcephalosporin C acetyltransferase (DAC-Soak)
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