4dc0: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dc0]] is a 2 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=4DC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DC0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dc0]] is a 2 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=4DC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DC0 FirstGlance]. <br>
</td></tr><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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.813&#8491;</td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dc0 OCA], [https://pdbe.org/4dc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dc0 RCSB], [https://www.ebi.ac.uk/pdbsum/4dc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dc0 ProSAT]</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=4dc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dc0 OCA], [https://pdbe.org/4dc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dc0 RCSB], [https://www.ebi.ac.uk/pdbsum/4dc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dc0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ACT3_STRCO ACT3_STRCO]]
[https://www.uniprot.org/uniprot/ACT3_STRCO ACT3_STRCO]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In the actinorhodin type II polyketide synthase, the first polyketide modification is a regiospecific C9-carbonyl reduction, catalyzed by the ketoreductase (actKR). Our previous studies identified the actKR 94-PGG-96 motif as a determinant of stereospecificity. The molecular basis for reduction regiospecificity is, however, not well understood. In this study, we examined the activities of 20 actKR mutants through a combination of kinetic studies, PKS reconstitution, and structural analyses. Residues have been identified that are necessary for substrate interaction, and these observations have suggested a structural model for this reaction. Polyketides dock at the KR surface and are steered into the enzyme pocket where C7-C12 cyclization is mediated by the KR before C9-ketoreduction can occur. These molecular features can potentially serve as engineering targets for the biosynthesis of novel, reduced polyketides.
 
The Determinants of Activity and Specificity in Actinorhodin Type II Polyketide Ketoreductase.,Javidpour P, Bruegger J, Srithahan S, Korman TP, Crump MP, Crosby J, Burkart MD, Tsai SC Chem Biol. 2013 Oct 24;20(10):1225-34. doi: 10.1016/j.chembiol.2013.07.016. Epub , 2013 Sep 12. PMID:24035284<ref>PMID:24035284</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4dc0" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 10:44, 1 March 2024

Crystal Structure of F189W Actinorhodin Polyketide Ketoreductase with NADPH

4dc0, resolution 2.81Å

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