1oc2

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spinqualitylabelsall models 1oc2, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

THE STRUCTURE OF NADH IN THE DTDP-D-GLUCOSE DEHYDRATASE (RMLB) ENZYME

Overview

The structure of Streptococcus suis serotype type 2 dTDP-d-glucose, 4,6-dehydratase (RmlB) has been determined to 1.5 A resolution with its, nicotinamide coenzyme and substrate analogue dTDP-xylose bound in an, abortive complex. During enzyme turnover, NAD(+) abstracts a hydride from, the C4' atom of dTDP-glucose-forming NADH. After elimination of water, hydride is then transferred back to the C6' atom of, dTDP-4-keto-5,6-glucosene-regenerating NAD(+). Single-crystal, spectroscopic studies unambiguously show that the coenzyme has been, trapped as NADH in the crystal. Electron density clearly demonstrates that, in contrast to native structures of RmlB where a flat nicotinamide ring is, observed, the dihydropyridine ring of the reduced cofactor in this complex, is found as a boat. The si ... [(full description)]

About this Structure

1OC2 is a [Single protein] structure of sequence from [Streptococcus suis] with SO4, TDX and NAD as [ligands]. Active as [dTDP-glucose 4,6-dehydratase], with EC number [4.2.1.46]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

The structure of NADH in the enzyme dTDP-d-glucose dehydratase (RmlB)., Beis K, Allard ST, Hegeman AD, Murshudov G, Philp D, Naismith JH, J Am Chem Soc. 2003 Oct 1;125(39):11872-8. PMID:14505409

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