5l45: Difference between revisions

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'''Unreleased structure'''


The entry 5l45 is ON HOLD  until Paper Publication
==polyketide ketoreductase SimC7 - apo crystal form 2==
<StructureSection load='5l45' size='340' side='right' caption='[[5l45]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5l45]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L45 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L45 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></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=5l45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l45 OCA], [http://pdbe.org/5l45 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l45 RCSB], [http://www.ebi.ac.uk/pdbsum/5l45 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l45 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
SimC7 is a polyketide ketoreductase involved in biosynthesis of the angucyclinone moiety of the gyrase inhibitor simocyclinone D8 (SD8). SimC7, which belongs to the short-chain dehydrogenase/reductase (SDR) superfamily, catalyzes reduction of the C-7 carbonyl of the angucyclinone, and the resulting hydroxyl is essential for antibiotic activity. SimC7 shares little sequence similarity with characterized ketoreductases, suggesting it might have a distinct mechanism. To investigate this possibility, we determined the structures of SimC7 alone, with NADP(+), and with NADP(+) and the substrate 7-oxo-SD8. These structures show that SimC7 is distinct from previously characterized polyketide ketoreductases, lacking the conserved catalytic triad, including the active-site tyrosine that acts as central acid-base catalyst in canonical SDR proteins. Taken together with functional analyses of active-site mutants, our data suggest that SimC7 catalyzes a substrate-assisted, two-step reaction for reduction of the C-7 carbonyl group involving intramolecular transfer of a substrate-derived proton to generate a phenolate intermediate.


Authors:  
Substrate-Assisted Catalysis in Polyketide Reduction Proceeds via a Phenolate Intermediate.,Schafer M, Stevenson CE, Wilkinson B, Lawson DM, Buttner MJ Cell Chem Biol. 2016 Sep 22;23(9):1091-7. doi: 10.1016/j.chembiol.2016.07.018., Epub 2016 Sep 8. PMID:27617849<ref>PMID:27617849</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5l45" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Buttner, M J]]
[[Category: Lawson, D M]]
[[Category: Schafer, M]]
[[Category: Stevenson, C E.M]]
[[Category: Wilkinson, B]]
[[Category: Dna gyrase inhibitor]]
[[Category: Hydrolase]]
[[Category: Ketoreductase]]
[[Category: Short-chain dehydrogenase/reductase]]
[[Category: Simocyclinone]]
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