2fr0
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(New page: 200px<br /><applet load="2fr0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fr0, resolution 1.81Å" /> '''The first ketoreduct...)
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Revision as of 08:35, 21 November 2007
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The first ketoreductase of the erythromycin synthase (crystal form 1)
Overview
The structure of the ketoreductase (KR) from the first module of the, erythromycin synthase with NADPH bound was solved to 1.79 A resolution., The 51 kDa domain has two subdomains, each similar to a short-chain, dehydrogenase/reductase (SDR) monomer. One subdomain has a truncated, Rossmann fold and serves a purely structural role stabilizing the other, subdomain, which catalyzes the reduction of the beta-carbonyl of a, polyketide and possibly the epimerization of an alpha-substituent. The, structure enabled us to define the domain boundaries of KR, the, dehydratase (DH), and the enoylreductase (ER). It also constrains the, three-dimensional organization of these domains within a module, revealing, that KR does not make dimeric contacts across the 2-fold axis of the, module. The quaternary structure elucidates how substrates are shuttled, between the active sites of polyketide synthases (PKSs), as well as, related fatty acid synthases (FASs), and suggests how domains can be, swapped to make hybrid synthases that produce novel polyketides.
About this Structure
2FR0 is a Single protein structure of sequence from Saccharopolyspora erythraea with NDP as ligand. Active as [acyl-carrier-protein_reductase 3-oxoacyl-[acyl-carrier-protein] reductase], with EC number 1.1.1.100 Full crystallographic information is available from OCA.
Reference
The structure of a ketoreductase determines the organization of the beta-carbon processing enzymes of modular polyketide synthases., Keatinge-Clay AT, Stroud RM, Structure. 2006 Apr;14(4):737-48. Epub 2006 Mar 23. PMID:16564177 [[Category: 3-oxoacyl-[acyl-carrier-protein] reductase]]
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