Document Detail


Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1.
MedLine Citation:
PMID:  15342255     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Biphenyl dioxygenase is the enzyme that catalyzes the stereospecific dioxygenation of the aromatic ring. This enzyme has attracted the attention of researchers due to its ability to oxidize polychlorinated biphenyls, which is one of the serious environmental contaminants. We determined the crystal structure of the terminal oxygenase component of the biphenyl dioxygenase (BphA1A2) derived from Rhodococcus strain sp. RHA1 in substrate-free and complex forms. These crystal structures revealed that the substrate-binding pocket makes significant conformational changes upon substrate binding to accommodate the substrate into the pocket. Our analysis of the crystal structures suggested that the residues in the substrate-binding pocket can be classified into three groups, which, respectively, seem to be responsible for the catalytic reaction, the orientation/conformation of the substrate, and the conformational changes of the substrate-binding pocket. The cooperative actions of residues in the three groups seem to determine the substrate specificity of the enzyme.
Authors:
Yutaka Furusawa; Venugopalan Nagarajan; Masaru Tanokura; Eiji Masai; Masao Fukuda; Toshiya Senda
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of molecular biology     Volume:  342     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2004 Sep 
Date Detail:
Created Date:  2004-09-02     Completed Date:  2004-10-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1041-52     Citation Subset:  IM    
Affiliation:
Biological Information Research Center (BIRC), National Institute of Advanced Industrial Science and Technology (AIST), 2-41-6 Aomi, Koto-ku, Tokyo 135-0064, Japan.
Data Bank Information
Bank Name/Acc. No.:
PDB/1ULI;  1ULJ
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Proteins / chemistry,  genetics,  metabolism
Catalytic Domain
Crystallography, X-Ray
Electron Transport Complex III / chemistry,  genetics,  metabolism
Environmental Pollutants / metabolism
Iron-Sulfur Proteins / chemistry,  genetics,  metabolism
Models, Molecular
Molecular Sequence Data
Oxidation-Reduction
Oxygenases / chemistry*,  genetics,  metabolism
Polychlorinated Biphenyls / metabolism
Protein Conformation
Rhodococcus / enzymology*,  genetics
Sequence Homology, Amino Acid
Substrate Specificity
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Environmental Pollutants; 0/Iron-Sulfur Proteins; 0/Polychlorinated Biphenyls; 0/Rieske iron-sulfur protein; EC 1.10.2.2/Electron Transport Complex III; EC 1.13.-/Oxygenases; EC 1.14.-/biphenyl-1,2-dioxygenase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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