5ydm: Difference between revisions

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New page: '''Unreleased structure''' The entry 5ydm is ON HOLD Authors: Li, Y., Qu, X.D., Zhou, J.H. Description: The crystal structure of the Acyl Transferase domain of SpnD complex with benzyl...
 
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'''Unreleased structure'''


The entry 5ydm is ON HOLD
==The crystal structure of the Acyl Transferase domain of SpnD complex with benzylmalonyl==
<StructureSection load='5ydm' size='340' side='right'caption='[[5ydm]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ydm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._CNQ431 Streptomyces sp. CNQ431]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YDM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YDM 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=DUW:(2~{R})-2-methanoyl-3-phenyl-propanoic+acid'>DUW</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=5ydm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ydm OCA], [https://pdbe.org/5ydm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ydm RCSB], [https://www.ebi.ac.uk/pdbsum/5ydm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ydm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0E3JLZ0_9ACTN A0A0E3JLZ0_9ACTN]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Polyketides are a large family of pharmaceutically important natural products, and the structural modification of their scaffolds is significant for drug development. Herein, we report high-resolution X-ray crystal structures of the broadly selective acyltransferase (AT) from the splenocin polyketide synthase (SpnD-AT) in the apo form and in complex with benzylmalonyl and pentynylmalonyl extender unit mimics. These structures revealed the molecular basis for the stereoselectivity and substrate specificity of SpnD-AT, and enabled the engineering of the industrially important Ery-AT6 to broaden its substrate scope to include three new types of extender units.


Authors: Li, Y., Qu, X.D., Zhou, J.H.
Structural Basis of a Broadly Selective Acyltransferase from the Polyketide Synthase of Splenocin.,Li Y, Zhang W, Zhang H, Tian W, Wu L, Wang S, Zheng M, Zhang J, Sun C, Deng Z, Sun Y, Qu X, Zhou J Angew Chem Int Ed Engl. 2018 May 14;57(20):5823-5827. doi:, 10.1002/anie.201802805. Epub 2018 Apr 14. PMID:29536601<ref>PMID:29536601</ref>


Description: The crystal structure of the Acyl Transferase domain of SpnD complex with benzylmalonyl
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Li, Y]]
<div class="pdbe-citations 5ydm" style="background-color:#fffaf0;"></div>
[[Category: Zhou, J.H]]
== References ==
[[Category: Qu, X.D]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces sp. CNQ431]]
[[Category: Li Y]]
[[Category: Qu XD]]
[[Category: Zhou JH]]
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