2wds

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[[Image:2wds.png|left|200px]]
 
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==Crystal structure of the Streptomyces coelicolor H110A AcpS mutant in complex with cofactor CoA at 1.3 A==
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The line below this paragraph, containing "STRUCTURE_2wds", creates the "Structure Box" on the page.
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<StructureSection load='2wds' size='340' side='right'caption='[[2wds]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2wds]] 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=2WDS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WDS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.35&#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=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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{{STRUCTURE_2wds| PDB=2wds | SCENE= }}
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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=2wds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wds OCA], [https://pdbe.org/2wds PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wds RCSB], [https://www.ebi.ac.uk/pdbsum/2wds PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wds 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/2wds_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=2wds 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 STREPTOMYCES COELICOLOR H110A ACPS MUTANT IN COMPLEX WITH COFACTOR COA AT 1.3 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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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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<div class="pdbe-citations 2wds" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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[[2wds]] is a 1 chain structure 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=2WDS OCA].
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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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<references/>
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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 Streptomyces coelicolor H110A AcpS mutant in complex with cofactor CoA at 1.3 A

PDB ID 2wds

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