1gkp
From Proteopedia
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==Overview== | ==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 ... | + | 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== | ==About this Structure== | ||
| - | 1GKP is a | + | 1GKP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_sp. Thermus sp.] with ZN, SO4 and EPE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Dihydropyrimidinase Dihydropyrimidinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.2 3.5.2.2] Structure known Active Site: ASA. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GKP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:30:30 2007'' |
Revision as of 10:25, 5 November 2007
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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 Structure known Active Site: ASA. 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
Page seeded by OCA on Mon Nov 5 12:30:30 2007
Categories: Dihydropyrimidinase | Single protein | Thermus sp. | Abendroth, J. | Niefind, K. | Schomburg, D. | EPE | SO4 | ZN | Cyclic amidase | Hydantoinase | Hydrolase
