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Structural assembly of the active site in an aldo-keto reductase by NADPH cofactor.

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Sanli G,Blaber M

doi

10.1006/jmbi.2001.4739

keywords:

subject

Has Abstract

pub_date

2001-06-22 00:00:00

pages

1209-18

issue

5

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(01)94739-4

journal_volume

309

pub_type

杂志文章

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