1HW6

CRYSTAL STRUCTURE OF APO-2,5-DIKETO-D-GLUCONATE REDUCTASE

Summary for 1HW6

• Entry DOI: 10.2210/pdb1hw6/pdb
• Related: 1A80
• Descriptor: 2,5-DIKETO-D-GLUCONIC ACID REDUCTASE, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: aldo-keto reductase, tim barrel, oxidoreductase
• Biological source: Corynebacterium sp.
• Cellular location: Cytoplasm: P06632
• Total number of polymer chains: 1
• Total formula weight: 30271.18

Authors

Sanli, G.,Blaber, M. (deposition date: 2001-01-09, release date: 2001-06-20, Last modification date: 2023-08-09)

Primary citation

Sanli, G.,Blaber, M.
Structural assembly of the active site in an aldo-keto reductase by NADPH cofactor.
J.Mol.Biol., 309:1209-1218, 2001

PubMed Abstract: 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.

PubMed: 11399090
DOI: 10.1006/jmbi.2001.4739

Experimental method

X-RAY DIFFRACTION (1.9 Å)