| 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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@article{342723,
author = {Marek, Jaromír and Vévodová, Jitka and KutáandSmatanová, Ivana and Nagata, Y. and Svensson, L.A. and Newman, J. and Takagi, M. and Damborský, Jiří},
article_location = {Washington, DC, USA},
article_number = {46},
keywords = {Crystal structure; haloalkane dehalogenase},
language = {eng},
issn = {0006-2960},
journal = {Biochemistry},
title = {Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26},
url = {http://www.ncbr.chemi.muni.cz/~jiri/ABSTRACTS/biochem00.html},
volume = {39},
year = {2000}
}
TY - JOUR
ID - 342723
AU - Marek, Jaromír - Vévodová, Jitka - Kutá-Smatanová, Ivana - Nagata, Y. - Svensson, L.A. - Newman, J. - Takagi, M. - Damborský, Jiří
PY - 2000
TI - Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26
JF - Biochemistry
VL - 39
IS - 46
SP - 14082
EP - 14082
PB - American Chemical Society
SN - 00062960
KW - Crystal structure
KW - haloalkane dehalogenase
UR - http://www.ncbr.chemi.muni.cz/~jiri/ABSTRACTS/biochem00.html
N2 - 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.
ER -
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. \textit{Biochemistry}. Washington, DC, USA: American Chemical Society, 2000, vol.~39, No~46, p.~14082-14086. ISSN~0006-2960.
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