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Functional annotation and three-dimensional structure of Dr0930 from Deinococcus radiodurans, a close relative of phosphotriesterase in the amidohydrolase superfamily.

Xiang, Dao Feng and Kolb, Peter and Fedorov, Alexander A. and Meier, Monika M. and Fedorov, Lena V. and Nguyen, T. Tinh and Sterner, Reinhard and Almo, Steven C. and Shoichet, Brian K. and Raushel, Frank M. (2009) Functional annotation and three-dimensional structure of Dr0930 from Deinococcus radiodurans, a close relative of phosphotriesterase in the amidohydrolase superfamily. Biochemistry 48 (10), pp. 2237-47.

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Abstract

Dr0930, a member of the amidohydrolase superfamily in Deinococcus radiodurans, was cloned, expressed, and purified to homogeneity. The enzyme crystallized in the space group P3121, and the structure was determined to a resolution of 2.1 A. The protein folds as a (beta/alpha)7beta-barrel, and a binuclear metal center is found at the C-terminal end of the beta-barrel. The purified protein contains ...

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Item Type:Article
Date:2009
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
19159332PubMed ID
10.1021/bi802274fDOI
Classification:
NotationType
Amidohydrolases/metabolismMESH
Amino Acid SequenceMESH
Amino Acid Substitution/physiologyMESH
BiocatalysisMESH
Catalytic DomainMESH
Crystallography, X-RayMESH
Deinococcus/geneticsMESH
Hydrogen BondingMESH
HydrophobicityMESH
KineticsMESH
Lactones/chemistryMESH
Metals, Heavy/chemistryMESH
Models, MolecularMESH
Molecular Sequence DataMESH
Phosphoric Triester Hydrolases/metabolismMESH
Protein ConformationMESH
Protein MultimerizationMESH
Pseudomonas/geneticsMESH
Recombinant Fusion Proteins/geneticsMESH
Recombinant Proteins/metabolismMESH
SpectrophotometryMESH
Static ElectricityMESH
Structural Homology, ProteinMESH
Substrate SpecificityMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Owner: Universitätsbibliothek Regensburg
Deposited On:22 Mar 2010 07:33
Last Modified:22 Mar 2010 09:53
Item ID:13667
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