2vav

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:31, 6 November 2024) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2vav.png|left|200px]]
 
-
{{STRUCTURE_2vav| PDB=2vav | SCENE= }}
+
==Crystal structure of deacetylcephalosporin C acetyltransferase (DAC-Soak)==
 +
<StructureSection load='2vav' size='340' side='right'caption='[[2vav]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2vav]] 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=2VAV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VAV FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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>, <scene name='pdbligand=OAS:O-ACETYLSERINE'>OAS</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vav OCA], [https://pdbe.org/2vav PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vav RCSB], [https://www.ebi.ac.uk/pdbsum/2vav PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vav ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CEFG_HAPCH CEFG_HAPCH] Catalyzes the conversion of deacetylcephalosporin C to cephalosporin C.<ref>PMID:1569032</ref>
 +
== 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/initialview03.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.
-
===CRYSTAL STRUCTURE OF DEACETYLCEPHALOSPORIN C ACETYLTRANSFERASE (DAC-SOAK)===
+
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>
-
{{ABSTRACT_PUBMED_18279889}}
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
==About this Structure==
+
<div class="pdbe-citations 2vav" style="background-color:#fffaf0;"></div>
-
[[2vav]] 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=2VAV OCA].
+
== References ==
-
 
+
<references/>
-
==Reference==
+
__TOC__
-
<ref group="xtra">PMID:018279889</ref><references group="xtra"/>
+
</StructureSection>
[[Category: Acremonium chrysogenum]]
[[Category: Acremonium chrysogenum]]
-
[[Category: Deacetylcephalosporin-C acetyltransferase]]
+
[[Category: Large Structures]]
-
[[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]]
+

Current revision

Crystal structure of deacetylcephalosporin C acetyltransferase (DAC-Soak)

PDB ID 2vav

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vav"
Personal tools