1hw6
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(New page: 200px<br /><applet load="1hw6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hw6, resolution 1.90Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 14:44, 20 November 2007
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CRYSTAL STRUCTURE OF APO-2,5-DIKETO-D-GLUCONATE REDUCTASE
Overview
A 1.9 A resolution X-ray structure of the apo-form of Corynebacterium, 2,5-diketo-d-gluconic acid reductase A (2,5-DKGR A), a member of the, aldo-keto reductase superfamily, has been determined by molecular, replacement using the NADPH-bound form of the same enzyme as the search, model. 2,5-DKGR A catalyzes the NADPH-dependent stereo-specific reduction, of 2,5-diketo-d-gluconate (2,5-DKG) to 2-keto-l-gulonate, a precursor in, the industrial production of vitamin C. An atomic-resolution structure for, the apo-form of the enzyme, in conjunction with our previously reported, high-resolution X-ray structure for the holo-enzyme and holo/substrate, model, allows a comparative analysis of structural changes that accompany, cofactor binding. The results show that regions of the active site undergo, coordinated conformational changes of up to 8 A. These conformational, changes result in the organization and structural rearrangement of, residues associated with substrate binding and catalysis. Thus, NADPH, functions not only to provide a hydride ion for catalytic reduction, but, is also a critical structural component for formation of a catalytically, competent form of DKGR A.
About this Structure
1HW6 is a Single protein structure of sequence from Corynebacterium sp. with MG and CL as ligands. Full crystallographic information is available from OCA.
Reference
Structural assembly of the active site in an aldo-keto reductase by NADPH cofactor., Sanli G, Blaber M, J Mol Biol. 2001 Jun 22;309(5):1209-18. PMID:11399090
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