2wdo

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[[Image:2wdo.png|left|200px]]
 
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{{STRUCTURE_2wdo| PDB=2wdo | SCENE= }}
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==Crystal structure of the S. coelicolor AcpS in complex with acetyl- CoA at 1.5 A==
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<StructureSection load='2wdo' size='340' side='right'caption='[[2wdo]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2wdo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WDO 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]] 1.56&#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=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2wdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wdo OCA], [https://pdbe.org/2wdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wdo RCSB], [https://www.ebi.ac.uk/pdbsum/2wdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wdo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ACPS_STRCO ACPS_STRCO] Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.[HAMAP-Rule:MF_00101]
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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/wd/2wdo_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=2wdo 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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The transfer of the phosphopantetheine chain from coenzyme A (CoA) to the acyl carrier protein (ACP), a key protein in both fatty acid and polyketide synthesis, is catalyzed by ACP synthase (AcpS). Streptomyces coelicolor AcpS is a doubly promiscuous enzyme capable of activation of ACPs from both fatty acid and polyketide synthesis and catalyzes the transfer of modified CoA substrates. Five crystal structures have been determined, including those of ligand-free AcpS, complexes with CoA and acetyl-CoA, and two of the active site mutants, His110Ala and Asp111Ala. All five structures are trimeric and provide further insight into the mechanism of catalysis, revealing the first detailed structure of a group I active site with the essential magnesium in place. Modeling of ACP binding supported by mutational analysis suggests an explanation for the promiscuity in terms of both ACP partner and modified CoA substrates.
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===CRYSTAL STRUCTURE OF THE S. COELICOLOR ACPS IN COMPLEX WITH ACETYL-COA AT 1.5 A===
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Analysis of Streptomyces coelicolor phosphopantetheinyl transferase, AcpS, reveals the basis for relaxed substrate specificity.,Dall'aglio P, Arthur CJ, Williams C, Vasilakis K, Maple HJ, Crosby J, Crump MP, Hadfield AT Biochemistry. 2011 Jun 28;50(25):5704-17. Epub 2011 Jun 6. PMID:21595442<ref>PMID:21595442</ref>
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{{ABSTRACT_PUBMED_21595442}}
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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 2wdo" style="background-color:#fffaf0;"></div>
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[[2wdo]] is a 1 chain structure of [[Acyl carrier protein synthase]] with sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WDO OCA].
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==See Also==
==See Also==
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*[[Acyl carrier protein synthase|Acyl carrier protein synthase]]
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*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:021595442</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Streptomyces coelicolor]]
[[Category: Streptomyces coelicolor]]
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[[Category: Aglio, P Dall.]]
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[[Category: Arthur C]]
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[[Category: Arthur, C.]]
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[[Category: Crosby J]]
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[[Category: Crosby, J.]]
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[[Category: Crump MP]]
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[[Category: Crump, M P.]]
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[[Category: Dall'Aglio P]]
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[[Category: Hadfield, A T.]]
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[[Category: Hadfield AT]]
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[[Category: Fatty acid biosynthesis]]
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[[Category: Lipid synthesis]]
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[[Category: Phosphopantetheine arm]]
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[[Category: Polyketide]]
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[[Category: Transferase]]
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Current revision

Crystal structure of the S. coelicolor AcpS in complex with acetyl- CoA at 1.5 A

PDB ID 2wdo

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