Crystal structure of the cold-adapted haloalkane dehalogenase
DpcA from Psychrobacter cryohalolentis K5

J 2019

Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5

TRATSIAK, K., Tanyana PRUDNIKOVA, Ivana DRIENOVSKÁ, Jiří DAMBORSKÝ, Jiří BRYNDA et. al.

Základní údaje

Originální název

Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5

Autoři

TRATSIAK, K., Tanyana PRUDNIKOVA (112 Bělorusko), Ivana DRIENOVSKÁ (703 Slovensko, domácí), Jiří DAMBORSKÝ (203 Česká republika, domácí), Jiří BRYNDA (203 Česká republika), Petr PACHL (203 Česká republika), Michal KUTÝ (203 Česká republika), Radka CHALOUPKOVÁ (203 Česká republika, garant, domácí), P. REZACOVA a I.K. SMATANOVA

Vydání

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, CHESTER, INT UNION CRYSTALLOGRAPHY, 2019, 2053-230X

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10609 Biochemical research methods

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 0.968

Kód RIV

RIV/00216224:14310/19:00108194

Organizační jednotka

Přírodovědecká fakulta

DOI

http://dx.doi.org/10.1107/S2053230X19002796

UT WoS

000466795900002

Klíčová slova anglicky

haloalkane dehalogenase; alpha/beta-hydrolase; X-ray diffraction; psychrophiles; structural analysis; Psychrobacter cryohalolentis

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 16. 2. 2023 12:24, Mgr. Michaela Hylsová, Ph.D.

Anotace

V originále

Haloalkane dehalogenases (HLDs) convert halogenated aliphatic pollutants to less toxic compounds by a hydrolytic mechanism. Owing to their broad substrate specificity and high enantioselectivity, haloalkane dehalogenases can function as biosensors to detect toxic compounds in the environment or can be used for the production of optically pure compounds. Here, the structural analysis of the haloalkane dehalogenase DpcA isolated from the psychrophilic bacterium Psychrobacter cryohalolentis K5 is presented at the atomic resolution of 1.05 angstrom. This enzyme exhibits a low temperature optimum, making it attractive for environmental applications such as biosensing at the subsurface environment, where the temperature typically does not exceed 25 degrees C. The structure revealed that DpcA possesses the shortest access tunnel and one of the most widely open main tunnels among structural homologs of the HLD-I subfamily. Comparative analysis revealed major differences in the region of the alpha 4 helix of the cap domain, which is one of the key determinants of the anatomy of the tunnels. The crystal structure of DpcA will contribute to better understanding of the structure-function relationships of cold-adapted enzymes.

Návaznosti

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

Citovat

TRATSIAK, K., Tanyana PRUDNIKOVA, Ivana DRIENOVSKÁ, Jiří DAMBORSKÝ, Jiří BRYNDA, Petr PACHL, Michal KUTÝ, Radka CHALOUPKOVÁ, P. REZACOVA a I.K. SMATANOVA. Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS. CHESTER: INT UNION CRYSTALLOGRAPHY, 2019, roč. 75, MAY 2019, s. 324-331. ISSN 2053-230X. Dostupné z: https://dx.doi.org/10.1107/S2053230X19002796.

@article{1638976,
   author = {Tratsiak, K. and Prudnikova, Tanyana and Drienovská, Ivana and Damborský, Jiří and Brynda, Jiří and Pachl, Petr and Kutý, Michal and Chaloupková, Radka and Rezacova, P. and Smatanova, I.K.},
   article_location = {CHESTER},
   article_number = {MAY 2019},
   doi = {http://dx.doi.org/10.1107/S2053230X19002796},
   keywords = {haloalkane dehalogenase; alpha/beta-hydrolase; X-ray diffraction; psychrophiles; structural analysis; Psychrobacter cryohalolentis},
   language = {eng},
   issn = {2053-230X},
   journal = {ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS},
   title = {Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5},
   url = {http://scripts.iucr.org/cgi-bin/paper?S2053230X19002796},
   volume = {75},
   year = {2019}
}

TY  - JOUR
ID  - 1638976
AU  - Tratsiak, K. - Prudnikova, Tanyana - Drienovská, Ivana - Damborský, Jiří - Brynda, Jiří - Pachl, Petr - Kutý, Michal - Chaloupková, Radka - Rezacova, P. - Smatanova, I.K.
PY  - 2019
TI  - Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5
JF  - ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
VL  - 75
IS  - MAY 2019
SP  - 324-331
EP  - 324-331
PB  - INT UNION CRYSTALLOGRAPHY
SN  - 2053230X
KW  - haloalkane dehalogenase
KW  - alpha/beta-hydrolase
KW  - X-ray diffraction
KW  - psychrophiles
KW  - structural analysis
KW  - Psychrobacter cryohalolentis
UR  - http://scripts.iucr.org/cgi-bin/paper?S2053230X19002796
L2  - http://scripts.iucr.org/cgi-bin/paper?S2053230X19002796
N2  - Haloalkane dehalogenases (HLDs) convert halogenated aliphatic pollutants to less toxic compounds by a hydrolytic mechanism. Owing to their broad substrate specificity and high enantioselectivity, haloalkane dehalogenases can function as biosensors to detect toxic compounds in the environment or can be used for the production of optically pure compounds. Here, the structural analysis of the haloalkane dehalogenase DpcA isolated from the psychrophilic bacterium Psychrobacter cryohalolentis K5 is presented at the atomic resolution of 1.05 angstrom. This enzyme exhibits a low temperature optimum, making it attractive for environmental applications such as biosensing at the subsurface environment, where the temperature typically does not exceed 25 degrees C. The structure revealed that DpcA possesses the shortest access tunnel and one of the most widely open main tunnels among structural homologs of the HLD-I subfamily. Comparative analysis revealed major differences in the region of the alpha 4 helix of the cap domain, which is one of the key determinants of the anatomy of the tunnels. The crystal structure of DpcA will contribute to better understanding of the structure-function relationships of cold-adapted enzymes.
ER  -

TRATSIAK, K., Tanyana PRUDNIKOVA, Ivana DRIENOVSKÁ, Jiří DAMBORSKÝ, Jiří BRYNDA, Petr PACHL, Michal KUTÝ, Radka CHALOUPKOVÁ, P. REZACOVA a I.K. SMATANOVA. Crystal structure of the cold-adapted haloalkane dehalogenase DpcA from Psychrobacter cryohalolentis K5. \textit{ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS}. CHESTER: INT UNION CRYSTALLOGRAPHY, 2019, roč.~75, MAY 2019, s.~324-331. ISSN~2053-230X. Dostupné z: https://dx.doi.org/10.1107/S2053230X19002796.

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