Crystal structure of the haloalkane dehalogenase from
Sphingomonas paucimobilis UT26

J 2000

Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26

MAREK, Jaromír, Jitka VÉVODOVÁ, Ivana KUTÁ-SMATANOVÁ, Y. NAGATA, L.A. SVENSSON et. al.

Základní údaje

Originální název

Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26

Autoři

MAREK, Jaromír (203 Česká republika, garant), Jitka VÉVODOVÁ (203 Česká republika, domácí), Ivana KUTÁ-SMATANOVÁ (203 Česká republika), Y. NAGATA, L.A. SVENSSON, J. NEWMAN, M. TAKAGI a Jiří DAMBORSKÝ (203 Česká republika)

Vydání

Biochemistry, Washington, DC, USA, American Chemical Society, 2000, 0006-2960

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.221

Kód RIV

RIV/00216224:14310/00:00002430

Organizační jednotka

Přírodovědecká fakulta

UT WoS

000165355700009

Klíčová slova anglicky

Crystal structure; haloalkane dehalogenase

Změněno: 2. 5. 2012 13:00, doc. RNDr. Jaromír Marek, Ph.D.

Anotace

V originále

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.

Návaznosti

MSM 143100005, záměr

Název: Strukturně-funkční vztahy biomolekul a jejich role v metabolismu

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Strukturně-funkční vztahy biomolekul a jejich role v metabolismu

Citovat

MAREK, Jaromír, Jitka VÉVODOVÁ, Ivana KUTÁ-SMATANOVÁ, Y. NAGATA, L.A. SVENSSON, J. NEWMAN, M. TAKAGI a Jiří DAMBORSKÝ. Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26. Biochemistry. Washington, DC, USA: American Chemical Society, 2000, roč. 39, č. 46, s. 14082-14086. ISSN 0006-2960.

@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 a Jiří DAMBORSKÝ. Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26. \textit{Biochemistry}. Washington, DC, USA: American Chemical Society, 2000, roč.~39, č.~46, s.~14082-14086. ISSN~0006-2960.

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