3slk
From Proteopedia
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| - | [[ | + | ==Structure of ketoreductase and enoylreductase didomain from modular polyketide synthase== |
| + | <StructureSection load='3slk' size='340' side='right' caption='[[3slk]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3slk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharopolyspora_spinosa Saccharopolyspora spinosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SLK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SLK 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spnB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=60894 Saccharopolyspora spinosa])</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=3slk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3slk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3slk RCSB], [http://www.ebi.ac.uk/pdbsum/3slk PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The enoylreductase (ER) is the final common enzyme from modular polyketide synthases (PKSs) to be structurally characterized. The 3.0 A-resolution structure of the didomain comprising the ketoreductase (KR) and ER from the second module of the spinosyn PKS reveals that ER shares an approximately 600-A(2) interface with KR distinct from that of the related mammalian fatty acid synthase (FAS). In contrast to the ER domains of the mammalian FAS, the ER domains of the second module of the spinosyn PKS do not make contact across the two-fold axis of the synthase. This monomeric organization may have been necessary in the evolution of multimodular PKSs to enable acyl carrier proteins to access each of their cognate enzymes. The isolated ER domain showed activity toward a substrate analog, enabling us to determine the contributions of its active site residues. | ||
| - | + | Divergence of multimodular polyketide synthases revealed by a didomain structure.,Zheng J, Gay DC, Demeler B, White MA, Keatinge-Clay AT Nat Chem Biol. 2012 May 27. doi: 10.1038/nchembio.964. PMID:22634636<ref>PMID:22634636</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Saccharopolyspora spinosa]] | [[Category: Saccharopolyspora spinosa]] | ||
| - | [[Category: Gay, D C | + | [[Category: Gay, D C]] |
| - | [[Category: Keatinge-Clay, A T | + | [[Category: Keatinge-Clay, A T]] |
| - | [[Category: Zheng, J | + | [[Category: Zheng, J]] |
[[Category: Nadph]] | [[Category: Nadph]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
Revision as of 14:13, 5 January 2015
Structure of ketoreductase and enoylreductase didomain from modular polyketide synthase
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