2vat: Difference between revisions

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{{Seed}}
[[Image:2vat.jpg|left|200px]]


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==Crystal structure of deacetylcephalosporin C acetyltransferase in complex with coenzyme A==
The line below this paragraph, containing "STRUCTURE_2vat", creates the "Structure Box" on the page.
<StructureSection load='2vat' size='340' side='right'caption='[[2vat]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_2vat|  PDB=2vat  |  SCENE=  }}
<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>
</table>
== Function ==
[https://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/2vat_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=2vat 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.


===CRYSTAL STRUCTURE OF DEACETYLCEPHALOSPORIN C ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A===
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2vat" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 18279889 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_18279889}}
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</StructureSection>
==About this Structure==
2VAT is a [[Single protein]] structure of 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].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/18279889 18279889]
[[Category: Acremonium chrysogenum]]
[[Category: Acremonium chrysogenum]]
[[Category: Deacetylcephalosporin-C acetyltransferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Ellis J]]
[[Category: Ellis, J.]]
[[Category: Lejon S]]
[[Category: Lejon, S.]]
[[Category: Valegard K]]
[[Category: Valegard, K.]]
[[Category: A/b- hydrolase fold]]
[[Category: Acetyl coenzyme some]]
[[Category: Acetyl transferase]]
[[Category: Acyltransferase]]
[[Category: Antibiotic biosynthesis]]
[[Category: Cephalosporin biosynthesis]]
[[Category: Transferase]]
 
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Retrieved from "https://proteopedia.org/2vat"