Differences in crystallization of two LinB variants from
Sphingobium japonicum UT26

J 2013

Differences in crystallization of two LinB variants from Sphingobium japonicum UT26

DEGTJARIK, O.; Radka CHALOUPKOVÁ; P. REZACOVA; M. KUTY; Jiří DAMBORSKÝ et al.

Základní údaje

Originální název

Differences in crystallization of two LinB variants from Sphingobium japonicum UT26

Autoři

DEGTJARIK, O.; Radka CHALOUPKOVÁ; P. REZACOVA; M. KUTY; Jiří DAMBORSKÝ a I. KUTA SMATANOVA

Vydání

Acta Crystallographica, 2013, 1744-3091

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

Impakt faktor

Impact factor: 0.568

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/13:00066680

Organizační jednotka

Přírodovědecká fakulta

DOI

https://doi.org/10.1107/S1744309113002467

UT WoS

000316745000014

Klíčová slova anglicky

Haloalkane dehalogenases

Štítky

AKR, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 29. 4. 2014 14:29, Ing. Zdeňka Rašková

Anotace

V originále

Haloalkane dehalogenases are microbial enzymes that convert a broad range of halogenated aliphatic compounds to their corresponding alcohols by the hydrolytic mechanism. These enzymes play an important role in the biodegradation of various environmental pollutants. Haloalkane dehalogenase LinB isolated from a soil bacterium Sphingobium japonicum UT26 has a relatively broad substrate specificity and can be applied in bioremediation and biosensing of environmental pollutants. The LinB variants presented here, LinB32 and LinB70, were constructed with the goal of studying the effect of mutations on enzyme functionality. In the case of LinB32 (L117W), the introduced mutation leads to blocking of the main tunnel connecting the deeply buried active site with the surrounding solvent. The other variant, LinB70 (L44I, H107Q), has the second halide-binding site in a position analogous to that in the related haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94. Both LinB variants were successfully crystallized and full data sets were collected for native enzymes as well as their complexes with the substrates 1,2-dibromoethane (LinB32) and 1-bromobutane (LinB70) to resolutions ranging from 1.6 to 2.8 A. The two mutants crystallize differently from each other, which suggests that the mutations, although deep inside the molecule, can still affect the protein crystallizability.

Návaznosti

GAP207/12/0775, projekt VaV

Název: Strukturně-funkční vztahy haloalkan dehalogenas

Investor: Grantová agentura ČR, Structure-functional Relationships of Haloalkane Dehalogenases

Citovat

DEGTJARIK, O.; Radka CHALOUPKOVÁ; P. REZACOVA; M. KUTY; Jiří DAMBORSKÝ a I. KUTA SMATANOVA. Differences in crystallization of two LinB variants from Sphingobium japonicum UT26. Acta Crystallographica. 2013, roč. 69, Pt 3, s. 284-287. ISSN 1744-3091. Dostupné z: https://doi.org/10.1107/S1744309113002467.

@article{1138872,
   author = {Degtjarik, O. and Chaloupková, Radka and Rezacova, P. and Kuty, M. and Damborský, Jiří and Kuta Smatanova, I.},
   article_number = {Pt 3},
   doi = {https://doi.org/10.1107/S1744309113002467},
   keywords = {Haloalkane dehalogenases},
   language = {eng},
   issn = {1744-3091},
   journal = {Acta Crystallographica},
   title = {Differences in crystallization of two LinB variants from Sphingobium japonicum UT26},
   volume = {69},
   year = {2013}
}

TY  - JOUR
ID  - 1138872
AU  - Degtjarik, O. - Chaloupková, Radka - Rezacova, P. - Kuty, M. - Damborský, Jiří - Kuta Smatanova, I.
PY  - 2013
TI  - Differences in crystallization of two LinB variants from Sphingobium japonicum UT26
JF  - Acta Crystallographica
VL  - 69
IS  - Pt 3
SP  - 284-287
EP  - 284-287
SN  - 17443091
KW  - Haloalkane dehalogenases
N2  - Haloalkane dehalogenases are microbial enzymes that convert a broad range of halogenated aliphatic compounds to their corresponding alcohols by the hydrolytic mechanism. These enzymes play an important role in the biodegradation of various environmental pollutants. Haloalkane dehalogenase LinB isolated from a soil bacterium Sphingobium japonicum UT26 has a relatively broad substrate specificity and can be applied in bioremediation and biosensing of environmental pollutants. The LinB variants presented here, LinB32 and LinB70, were constructed with the goal of studying the effect of mutations on enzyme functionality. In the case of LinB32 (L117W), the introduced mutation leads to blocking of the main tunnel connecting the deeply buried active site with the surrounding solvent. The other variant, LinB70 (L44I, H107Q), has the second halide-binding site in a position analogous to that in the related haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94. Both LinB variants were successfully crystallized and full data sets were collected for native enzymes as well as their complexes with the substrates 1,2-dibromoethane (LinB32) and 1-bromobutane (LinB70) to resolutions ranging from 1.6 to 2.8 A. The two mutants crystallize differently from each other, which suggests that the mutations, although deep inside the molecule, can still affect the protein crystallizability.
ER  -

DEGTJARIK, O.; Radka CHALOUPKOVÁ; P. REZACOVA; M. KUTY; Jiří DAMBORSKÝ a I. KUTA SMATANOVA. Differences in crystallization of two LinB variants from Sphingobium japonicum UT26. \textit{Acta Crystallographica}. 2013, roč.~69, Pt 3, s.~284-287. ISSN~1744-3091. Dostupné z: https://doi.org/10.1107/S1744309113002467.

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