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4hxy
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4hxy is ON HOLD until Paper Publication Authors: Whicher, J.R., Smith, J.L. Description: PlmKR1-Ketoreductase from the first module of phoslactomyc...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==PlmKR1-Ketoreductase from the first module of phoslactomycin biosynthesis in Streptomyces sp. HK803== | |
| + | <StructureSection load='4hxy' size='340' side='right'caption='[[4hxy]], [[Resolution|resolution]] 1.68Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4hxy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._HK803 Streptomyces sp. HK803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HXY 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]] 1.68Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACA:6-AMINOHEXANOIC+ACID'>ACA</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</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=4hxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hxy OCA], [https://pdbe.org/4hxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hxy RCSB], [https://www.ebi.ac.uk/pdbsum/4hxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hxy ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q6V1M8_9ACTN Q6V1M8_9ACTN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The formation of an activated cis-3-cyclohexylpropenoic acid by Plm1, the first extension module of the phoslactomycin polyketide synthase, is proposed to occur through an L-3-hydroxyacyl-intermediate as a result of ketoreduction by an A-type ketoreductase (KR). Here, we demonstrate that the KR domain of Plm1 (PlmKR1) catalyzes the formation of an L-3-hydroxyacyl product. The crystal structure of PlmKR1 revealed a well-ordered active site with a nearby Trp residue characteristic of A-type KRs. Structural comparison of PlmKR1 with B-type KRs that produce D-3-hydroxyacyl intermediates revealed significant differences. The active site of cofactor-bound A-type KRs is in a catalysis-ready state, whereas cofactor-bound B-type KRs are in a precatalytic state. Furthermore, the closed lid loop in substrate-bound A-type KRs restricts active site access from all but one direction, which is proposed to control the stereochemistry of ketoreduction. | ||
| - | + | Structural and Stereochemical Analysis of a Modular Polyketide Synthase Ketoreductase Domain Required for the Generation of a cis-Alkene.,Bonnett SA, Whicher JR, Papireddy K, Florova G, Smith JL, Reynolds KA Chem Biol. 2013 Jun 20;20(6):772-83. doi: 10.1016/j.chembiol.2013.04.014. PMID:23790488<ref>PMID:23790488</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4hxy" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces sp. HK803]] | ||
| + | [[Category: Smith JL]] | ||
| + | [[Category: Whicher JR]] | ||
Current revision
PlmKR1-Ketoreductase from the first module of phoslactomycin biosynthesis in Streptomyces sp. HK803
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