MAREK, Jaromír, Jitka VÉVODOVÁ, Ivana KUTÁ-SMATANOVÁ, Y. NAGATA, L.A. SVENSSON, J. NEWMAN, M. TAKAGI and Jiří DAMBORSKÝ. Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26. Biochemistry. Washington, DC, USA: American Chemical Society, 2000, vol. 39, No 46, p. 14082-14086. ISSN 0006-2960.
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Basic information
Original name Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26
Authors MAREK, Jaromír (203 Czech Republic, guarantor), Jitka VÉVODOVÁ (203 Czech Republic, belonging to the institution), Ivana KUTÁ-SMATANOVÁ (203 Czech Republic), Y. NAGATA, L.A. SVENSSON, J. NEWMAN, M. TAKAGI and Jiří DAMBORSKÝ (203 Czech Republic).
Edition Biochemistry, Washington, DC, USA, American Chemical Society, 2000, 0006-2960.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10600 1.6 Biological sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 4.221
RIV identification code RIV/00216224:14310/00:00002430
Organization unit Faculty of Science
UT WoS 000165355700009
Keywords in English Crystal structure; haloalkane dehalogenase
Changed by Changed by: doc. RNDr. Jaromír Marek, Ph.D., učo 1989. Changed: 2/5/2012 13:00.
Abstract
The haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB) is the enzyme involved in the degradation ofthe important environmental pollutant g-hexachlorocyclohexane. The enzyme hydrolyzes a broad range of halogenated cyclic and aliphatic compounds. Here, we present the 1.58 A crystal structure of LinB and the 2.0 A structure of LinB with 1,3-propanediol, a product of debromination of 1,3-dibromopropane, in the active site of the enzyme. The enzyme belongs to the a/b-hydrolase family and contains a catalytic triad (Aspl08, His272, and Glu132) in the lipase-like topological arrangement previously proposed from mutagenesis experiments. The LinB structure was compared with the structures of haloalkane dehalogenase from Xanthobacter autotrophicus GJl0 and from Rhodococcus sp. and the structural features involved in the adaptation toward xenobiotic substrates were identified. The arrangement and composition of the a-helices in the cap domain results in the dif ferences in the size and shape of the active-site cavity and the entrance tunnel. This is the major determinant ofthe substrate specificity ofthis haloalkane dehalogenase.
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MSM 143100005, plan (intention)Name: Strukturně-funkční vztahy biomolekul a jejich role v metabolismu
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular Structure-function Relationships and their role in the Metabolism
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