1rjw

From Proteopedia

Revision as of 06:33, 30 October 2007

CRYSTAL STRUCTURE OF NAD(+)-DEPENDENT ALCOHOL DEHYDROGENASE FROM BACILLUS STEAROTHERMOPHILUS STRAIN LLD-R

Overview

The crystal structure of NAD(+)-dependent alcohol dehydrogenase from, Bacillus stearothermophilus strain LLD-R (htADH) was determined using, X-ray diffraction data at a resolution of 2.35 A. The structure of, homotetrameric htADH is highly homologous to those of bacterial and, archaeal homotetrameric alcohol dehydrogenases (ADHs) and also to the, mammalian dimeric ADHs. There is one catalytic zinc atom and one, structural zinc atom per enzyme subunit. The enzyme was crystallized as a, binary complex lacking the nicotinamide adenine dinucleotide (NAD(+)), cofactor but including a zinc-coordinated substrate analogue, trifluoroethanol. The binary complex structure is in an open conformation, similar to ADH structures without the bound cofactor. Features important, for the thermostability of ... [(full description)]

About this Structure

1RJW is a [Single protein] structure of sequence from [Bacillus stearothermophilus] with ZN and ETF as [ligands]. Active as [Oxidoreductase], with EC number [1.1.1.1]. Structure known Active Site: ZN8. Full crystallographic information is available from [OCA].

Reference

Crystal structure and amide H/D exchange of binary complexes of alcohol dehydrogenase from Bacillus stearothermophilus: insight into thermostability and cofactor binding., Ceccarelli C, Liang ZX, Strickler M, Prehna G, Goldstein BM, Klinman JP, Bahnson BJ, Biochemistry. 2004 May 11;43(18):5266-77. PMID:15122892

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