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4j1q

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==Crystal structure of a ketoreductase domain from the bacillaene assembly line==
==Crystal structure of a ketoreductase domain from the bacillaene assembly line==
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<StructureSection load='4j1q' size='340' side='right' caption='[[4j1q]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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<StructureSection load='4j1q' size='340' side='right'caption='[[4j1q]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4j1q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J1Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4j1q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J1Q FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene><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]] 2.35&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j1s|4j1s]]</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=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU17180, pksJ, pksJ (amino acids 2669-3111), pksK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=4j1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j1q OCA], [https://pdbe.org/4j1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j1q RCSB], [https://www.ebi.ac.uk/pdbsum/4j1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j1q ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-oxoacyl-[acyl-carrier-protein]_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.100 1.1.1.100] </span></td></tr>
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</table>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4j1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j1q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j1q RCSB], [http://www.ebi.ac.uk/pdbsum/4j1q PDBsum]</span></td></tr>
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== Function ==
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<table>
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[https://www.uniprot.org/uniprot/PKSJ_BACSU PKSJ_BACSU] Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.<ref>PMID:16460000</ref> <ref>PMID:17234808</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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While the cis-acyltransferase modular polyketide synthase assembly lines have largely been structurally dissected, enzymes from within the recently discovered trans-acyltransferase polyketide synthase assembly lines are just starting to be observed crystallographically. Here we examine the ketoreductase (KR) from the first polyketide synthase module of the bacillaene nonribosomal peptide synthetase/polyketide synthase at 2.35-A resolution. This KR naturally reduces both alpha- and beta-keto groups and is the only KR known to do so during the biosynthesis of a polyketide. The isolated KR not only reduced an N-acetylcysteamine-bound beta-keto substrate to a D-beta-hydroxy product, but also an N-acetylcysteamine-bound alpha-keto substrate to an L-alpha-hydroxy product. That the substrates must enter the active site from opposite directions to generate these stereochemistries suggests that the acyl-phosphopantetheine moiety is capable of accessing very different conformations despite being anchored to a serine residue of a docked acyl carrier protein. The features enabling stereocontrolled alpha-ketoreduction may not be extensive since a KR that naturally reduces a beta-keto group within a cis-acyltransferase polyketide synthase was identified that performs a completely stereoselective reduction of the same alpha-keto substrate to generate the D-alpha-hydroxy product. A sequence analysis of trans-acyltransferase KRs reveals that a single residue, rather than a three-residue motif found in cis-acyltransferase KRs, is predictive of the orientation of the resulting beta-hydroxyl group.Proteins 2014. (c) 2014 Wiley Periodicals, Inc.
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Structural and functional studies of a trans-acyltransferase polyketide assembly line enzyme that catalyzes stereoselective alpha- and beta-ketoreduction.,Piasecki SK, Zheng J, Axelrod AJ, E Detelich M, Keatinge-Clay AT Proteins. 2014 Mar 14. doi: 10.1002/prot.24561. PMID:24634061<ref>PMID:24634061</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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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacsu]]
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[[Category: Bacillus subtilis subsp. subtilis str. 168]]
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[[Category: Keatinge-Clay, A T.]]
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[[Category: Large Structures]]
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[[Category: Zheng, J.]]
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[[Category: Keatinge-Clay AT]]
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[[Category: Ketoreductase]]
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[[Category: Zheng J]]
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[[Category: Oxidoreductase]]
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[[Category: Rossmann fold]]
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Current revision

Crystal structure of a ketoreductase domain from the bacillaene assembly line

PDB ID 4j1q

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