3qp9

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The Structure of a C2-type Ketoreductase from a Modular Polyketide Synthase

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Retrieved from "http://52.214.119.220/wiki/index.php/3qp9"

Categories: Large Structures | Streptomyces venezuelae | Keatinge-Clay AT | Zheng J

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 <StructureSection load='3qp9' size='340' side='right'caption='[[3qp9]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3qp9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/As_4.1526 As 4.1526]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QP9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3qp9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_venezuelae Streptomyces venezuelae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QP9 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pikAII ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=54571 AS 4.1526])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.88&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] </span></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=3qp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qp9 OCA], [https://pdbe.org/3qp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qp9 RCSB], [https://www.ebi.ac.uk/pdbsum/3qp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qp9 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/PIKA2_STRVZ PIKA2_STRVZ] Involved in the biosynthesis of 12- and 14-membered ring macrolactone antibiotics such as methymycin/neomethymycin and pikromycin/narbomycin, respectively. Component of the pikromycin PKS which catalyzes the biosynthesis of both precursors 10-deoxymethynolide (12-membered ring macrolactone) and narbonolide (14-membered ring macrolactone). Chain elongation through PikAI, PikAII and PikAIII followed by thioesterase catalyzed termination results in the production of 10-deoxymethynolide, while continued elongation through PikAIV, followed by thioesterase (TE) catalyzed cyclization results in the biosynthesis of the narbonolide.<ref>PMID:10421766</ref> <ref>PMID:21570406</ref> <ref>PMID:19027305</ref>
-The process by which alpha-stereocenters of polyketide intermediates are set by modular polyketide synthases (PKSs) when condensation is not immediately followed by reduction is mysterious. However, the reductase-incompetent ketoreductase (KR) from the third module of 6-deoxyerythronolide B synthase has been proposed to operate as a racemase, aiding in the epimerization process that reverses the orientation of the alpha-methyl group of the polyketide intermediate generated by the ketosynthase to the configuration observed in the 6-deoxyerythronolide B final product. To learn more about the epimerization process, the structure of the C2-type KR from the third module of the pikromycin synthase, analogous to the KR from the third module of 6-deoxyerythronolide B synthase, was determined to 1.88 A resolution. This first structural analysis of this KR-type reveals differences from reductase-competent KRs such as that the site NADPH binds to reductase-competent KRs is occluded by side chains and the putative catalytic tyrosine possesses more degrees of freedom. The active-site geometry may enable C2-type KRs to align the thioester and beta-keto groups of a polyketide intermediate to reduce the pK(a) of the alpha-proton and accelerate its abstraction. Results from in vivo assays of engineered PKSs support that C2-type KRs cooperate with epimer-specific ketosynthases to set the configurations of substituent-bearing alpha-carbons.
-Structural and functional analysis of c2-type ketoreductases from modular polyketide synthases.,Zheng J, Keatinge-Clay AT J Mol Biol. 2011 Jul 1;410(1):105-17. Epub 2011 May 5. PMID:21570406<ref>PMID:21570406</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3qp9" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: As 4 1526]]
 [[Category: Large Structures]]
-[[Category: Keatinge-Clay, A T]]
+[[Category: Streptomyces venezuelae]]
-[[Category: Zheng, J]]
+[[Category: Keatinge-Clay AT]]
-[[Category: Epimerization]]
+[[Category: Zheng J]]
-[[Category: Ketoreductase]]
-[[Category: Oxidoreductase]]
-[[Category: Rossmann fold]]

3qp9

From Proteopedia

Current revision

The Structure of a C2-type Ketoreductase from a Modular Polyketide Synthase

Structural highlights

Function

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