Crystallization and Crystallographic Analysis of a
Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant
with an Eliminated Halide-Binding Site

J 2019

Crystallization and Crystallographic Analysis of a Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant with an Eliminated Halide-Binding Site

PRUDNIKOVA, T., B. KASCAKOVA, J.R. MESTERS, P. GRINKEVICH, P. HAVLICKOVA et. al.

Základní údaje

Originální název

Crystallization and Crystallographic Analysis of a Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant with an Eliminated Halide-Binding Site

Autoři

PRUDNIKOVA, T., B. KASCAKOVA, J.R. MESTERS, P. GRINKEVICH, P. HAVLICKOVA, A. MAZUR, A. SHAPOSHNIKOVA, Radka CHALOUPKOVÁ (203 Česká republika, domácí), Jiří DAMBORSKÝ (203 Česká republika, garant, domácí), M. KUTY a I.K. SMATANOVA

Vydání

CRYSTALS, BASEL, MDPI, 2019, 2073-4352

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

20500 2.5 Materials engineering

Stát vydavatele

Švýcarsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 2.404

Kód RIV

RIV/00216224:14310/19:00108205

Organizační jednotka

Přírodovědecká fakulta

DOI

http://dx.doi.org/10.3390/cryst9070375

UT WoS

000482052800024

Klíčová slova anglicky

Haloalkane dehalogenase; halide-binding site; random microseeding

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 16. 2. 2023 12:26, Mgr. Michaela Hylsová, Ph.D.

Anotace

V originále

Haloalkane dehalogenases are a very important class of microbial enzymes for environmental detoxification of halogenated pollutants, for biocatalysis, biosensing and molecular tagging. The double mutant (Ile44Leu + Gln102His) of the haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94 (DbeA Delta Cl) was constructed to study the role of the second halide-binding site previously discovered in the wild-type structure. The variant is less active, less stable in the presence of chloride ions and exhibits significantly altered substrate specificity when compared with the DbeAwt. DbeA Delta Cl was crystallized using the sitting-drop vapour-diffusion procedure with further optimization by the random microseeding technique. The crystal structure of the DbeA Delta Cl has been determined and refined to the 1.4 angstrom resolution. The DbeA Delta Cl crystals belong to monoclinic space group C121. The DbeA Delta Cl molecular structure was characterized and compared with five known haloalkane dehalogenases selected from the Protein Data Bank.

Návaznosti

ED0001/01/01, projekt VaV

Název: CETOCOEN

GA17-24321S, projekt VaV

Název: Studium hydratace a flexibility enzymů pomocí pokročilých strukturních a biofyzikálních metod

Investor: Grantová agentura ČR, Studium hydratace a flexibility enzymů pomocí pokročilých strukturních a biofyzikálních metod

LM2015055, projekt VaV

Název: Centrum pro systémovou biologii (Akronym: C4SYS)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, The national infrastructure C4SYS - Centre for Systems Biology

Citovat

PRUDNIKOVA, T., B. KASCAKOVA, J.R. MESTERS, P. GRINKEVICH, P. HAVLICKOVA, A. MAZUR, A. SHAPOSHNIKOVA, Radka CHALOUPKOVÁ, Jiří DAMBORSKÝ, M. KUTY a I.K. SMATANOVA. Crystallization and Crystallographic Analysis of a Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant with an Eliminated Halide-Binding Site. CRYSTALS. BASEL: MDPI, 2019, roč. 9, č. 7, s. 1-12. ISSN 2073-4352. Dostupné z: https://dx.doi.org/10.3390/cryst9070375.

@article{1639538,
   author = {Prudnikova, T. and Kascakova, B. and Mesters, J.R. and Grinkevich, P. and Havlickova, P. and Mazur, A. and Shaposhnikova, A. and Chaloupková, Radka and Damborský, Jiří and Kuty, M. and Smatanova, I.K.},
   article_location = {BASEL},
   article_number = {7},
   doi = {http://dx.doi.org/10.3390/cryst9070375},
   keywords = {Haloalkane dehalogenase; halide-binding site; random microseeding},
   language = {eng},
   issn = {2073-4352},
   journal = {CRYSTALS},
   title = {Crystallization and Crystallographic Analysis of a Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant with an Eliminated Halide-Binding Site},
   url = {http://dx.doi.org/10.3390/cryst9070375},
   volume = {9},
   year = {2019}
}

TY  - JOUR
ID  - 1639538
AU  - Prudnikova, T. - Kascakova, B. - Mesters, J.R. - Grinkevich, P. - Havlickova, P. - Mazur, A. - Shaposhnikova, A. - Chaloupková, Radka - Damborský, Jiří - Kuty, M. - Smatanova, I.K.
PY  - 2019
TI  - Crystallization and Crystallographic Analysis of a Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant with an Eliminated Halide-Binding Site
JF  - CRYSTALS
VL  - 9
IS  - 7
SP  - 1-12
EP  - 1-12
PB  - MDPI
SN  - 20734352
KW  - Haloalkane dehalogenase
KW  - halide-binding site
KW  - random microseeding
UR  - http://dx.doi.org/10.3390/cryst9070375
L2  - http://dx.doi.org/10.3390/cryst9070375
N2  - Haloalkane dehalogenases are a very important class of microbial enzymes for environmental detoxification of halogenated pollutants, for biocatalysis, biosensing and molecular tagging. The double mutant (Ile44Leu + Gln102His) of the haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94 (DbeA Delta Cl) was constructed to study the role of the second halide-binding site previously discovered in the wild-type structure. The variant is less active, less stable in the presence of chloride ions and exhibits significantly altered substrate specificity when compared with the DbeAwt. DbeA Delta Cl was crystallized using the sitting-drop vapour-diffusion procedure with further optimization by the random microseeding technique. The crystal structure of the DbeA Delta Cl has been determined and refined to the 1.4 angstrom resolution. The DbeA Delta Cl crystals belong to monoclinic space group C121. The DbeA Delta Cl molecular structure was characterized and compared with five known haloalkane dehalogenases selected from the Protein Data Bank.
ER  -

PRUDNIKOVA, T., B. KASCAKOVA, J.R. MESTERS, P. GRINKEVICH, P. HAVLICKOVA, A. MAZUR, A. SHAPOSHNIKOVA, Radka CHALOUPKOVÁ, Jiří DAMBORSKÝ, M. KUTY a I.K. SMATANOVA. Crystallization and Crystallographic Analysis of a Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant with an Eliminated Halide-Binding Site. \textit{CRYSTALS}. BASEL: MDPI, 2019, roč.~9, č.~7, s.~1-12. ISSN~2073-4352. Dostupné z: https://dx.doi.org/10.3390/cryst9070375.

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