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| | ==Crystal Structure of V151L Actinorhodin Polyketide Ketoreductase with NADPH== | | ==Crystal Structure of V151L Actinorhodin Polyketide Ketoreductase with NADPH== |
| - | <StructureSection load='4dbz' size='340' side='right' caption='[[4dbz]], [[Resolution|resolution]] 2.64Å' scene=''> | + | <StructureSection load='4dbz' size='340' side='right'caption='[[4dbz]], [[Resolution|resolution]] 2.64Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4dbz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DBZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DBZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4dbz]] 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=4DBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DBZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dc0|4dc0]], [[4dc1|4dc1]]</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=4dbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dbz OCA], [https://pdbe.org/4dbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dbz RCSB], [https://www.ebi.ac.uk/pdbsum/4dbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dbz ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">actIII, SCBAC28G1.12c, SCO5086 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1902 "Actinomyces coelicolor" (Muller 1908) Lieske 1921])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4dbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dbz OCA], [http://pdbe.org/4dbz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dbz RCSB], [http://www.ebi.ac.uk/pdbsum/4dbz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dbz ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/ACT3_STRCO ACT3_STRCO]] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Javidpour, P]] | + | [[Category: Large Structures]] |
| - | [[Category: Tsai, S C]] | + | [[Category: Streptomyces coelicolor]] |
| - | [[Category: Ketoreductase]] | + | [[Category: Javidpour P]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Tsai S-C]] |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
[ACT3_STRCO]
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Javidpour P, Bruegger J, Srithahan S, Korman TP, Crump MP, Crosby J, Burkart MD, Tsai SC. The Determinants of Activity and Specificity in Actinorhodin Type II Polyketide Ketoreductase. Chem Biol. 2013 Oct 24;20(10):1225-34. doi: 10.1016/j.chembiol.2013.07.016. Epub , 2013 Sep 12. PMID:24035284 doi:http://dx.doi.org/10.1016/j.chembiol.2013.07.016
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