1gkp

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spinqualitylabelsall models 1gkp, resolution 1.295Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

D-HYDANTOINASE (DIHYDROPYRIMIDINASE) FROM THERMUS SP. IN SPACE GROUP C2221

Overview

Dihydropyrimidinases (hydantoinases) catalyse the reversible hydrolytic, ring-opening of cyclic diamides such as dihydropyrimidines in the, catabolism of pyrimidines. In biotechnology, these enzymes find, application in the enantiospecific production of amino acids from racemic, hydantoins. The crystal structure of a D-enantio-specific, dihydropyrimidinase from Thermus sp. (D-hydantoinase) was solved de novo, by multiwavelength anomalous diffraction phasing. In spite of a large unit, cell the D-hydantoinase crystals exhibit excellent diffraction properties., The structure was subsequently refined at 1.30 A resolution against native, data. The core of D-hydantoinase consists of a (alpha/beta)(8)-barrel, which is flanked by a beta-sheet domain and some additional helices. In, the active site, a carboxylated lysine residue and the catalytically, active hydroxide ion bridge a binuclear zinc centre. The tertiary, structure and shape of the active site show strong homology to that of, ureases, dihydroorotases, and phosphotriesterases. The homology of the, active site was exploited for in silicio docking of substrates in the, active site. This could shed light both on the substrate binding in, hydantoinases and on the recently highly discussed origin of the proton in, the course of hydantoinase catalysis.

About this Structure

1GKP is a Single protein structure of sequence from Thermus sp. with ZN, SO4 and EPE as ligands. Active as Dihydropyrimidinase, with EC number 3.5.2.2 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

X-ray structure of a dihydropyrimidinase from Thermus sp. at 1.3 A resolution., Abendroth J, Niefind K, Schomburg D, J Mol Biol. 2002 Jun 28;320(1):143-56. PMID:12079340

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