From Proteopedia
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| - | [[Image:1gkp.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1gkp| PDB=1gkp | SCENE= }} | | {{STRUCTURE_1gkp| PDB=1gkp | SCENE= }} |
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| - | '''D-HYDANTOINASE (DIHYDROPYRIMIDINASE) FROM THERMUS SP. IN SPACE GROUP C2221'''
| + | ===D-HYDANTOINASE (DIHYDROPYRIMIDINASE) FROM THERMUS SP. IN SPACE GROUP C2221=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12079340}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12079340 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12079340}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hydantoinase]] | | [[Category: Hydantoinase]] |
| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:42:01 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:27:02 2008'' |
Revision as of 02:27, 1 July 2008
Template:STRUCTURE 1gkp
D-HYDANTOINASE (DIHYDROPYRIMIDINASE) FROM THERMUS SP. IN SPACE GROUP C2221
Template:ABSTRACT PUBMED 12079340
About this Structure
1GKP is a Single protein structure of sequence from Thermus sp.. 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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