5l40: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "5l40" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
==polyketide ketoreductase SimC7 - apo crystal form 1== | |||
<StructureSection load='5l40' size='340' side='right' caption='[[5l40]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5l40]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L40 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L40 FirstGlance]. <br> | |||
</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=5l40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l40 OCA], [http://pdbe.org/5l40 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l40 RCSB], [http://www.ebi.ac.uk/pdbsum/5l40 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l40 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5l40" 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: Ketoreductase]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Short-chain dehydrogenase/reductase]] | |||
[[Category: Simocyclinone]] | |||
Revision as of 21:35, 5 October 2016
polyketide ketoreductase SimC7 - apo crystal form 1
| ||||||||||||
