Deciphering the Structural Basis of High Thermostability of
Dehalogenase from Psychrophilic Bacterium Marinobacter sp.
ELB17

J 2019

Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17

CHRÁST, Lukáš, K. TRATSIAK, Joan PLANAS IGLESIAS, Lukáš DANIEL, T. PRUDNIKOVA et. al.

Basic information

Original name

Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17

Authors

CHRÁST, Lukáš (203 Czech Republic, belonging to the institution), K. TRATSIAK, Joan PLANAS IGLESIAS (724 Spain, belonging to the institution), Lukáš DANIEL (203 Czech Republic, belonging to the institution), T. PRUDNIKOVA, Jan BREZOVSKÝ (203 Czech Republic, belonging to the institution), David BEDNÁŘ (203 Czech Republic, belonging to the institution), I.K. SMATANOVA, Radka CHALOUPKOVÁ (203 Czech Republic, belonging to the institution) and Jiří DAMBORSKÝ (203 Czech Republic, guarantor, belonging to the institution)

Edition

Microorganisms, Basel, MDPI, 2019, 2076-2607

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10606 Microbiology

Country of publisher

Switzerland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 4.152

RIV identification code

RIV/00216224:14310/19:00108215

Organization unit

Faculty of Science

DOI

http://dx.doi.org/10.3390/microorganisms7110498

UT WoS

000502273600021

Keywords in English

haloalkane dehalogenase; thermostability; psychrophile; access tunnel; dimer; catalytic pentad; enantiselectivity

Abstract

V originále

Haloalkane dehalogenases are enzymes with a broad application potential in biocatalysis, bioremediation, biosensing and cell imaging. The new haloalkane dehalogenase DmxA originating from the psychrophilic bacterium Marinobacter sp. ELB17 surprisingly possesses the highest thermal stability (apparent melting temperature T-m,T-app = 65.9 degrees C) of all biochemically characterized wild type haloalkane dehalogenases belonging to subfamily II. The enzyme was successfully expressed and its crystal structure was solved at 1.45 angstrom resolution. DmxA structure contains several features distinct from known members of haloalkane dehalogenase family: (i) a unique composition of catalytic residues; (ii) a dimeric state mediated by a disulfide bridge; and (iii) narrow tunnels connecting the enzyme active site with the surrounding solvent. The importance of narrow tunnels in such paradoxically high stability of DmxA enzyme was confirmed by computational protein design and mutagenesis experiments.

Links

EF16_027/0008360, research and development project

Name: Postdoc@MUNI

GA17-24321S, research and development project

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

Investor: Czech Science Foundation

LM2015047, research and development project

Name: Česká národní infrastruktura pro biologická data (Acronym: ELIXIR-CZ)

Investor: Ministry of Education, Youth and Sports of the CR, Czech National Infrastructure for Biological Data

LM2015051, research and development project

Name: Centrum pro výzkum toxických látek v prostředí (Acronym: RECETOX RI)

Investor: Ministry of Education, Youth and Sports of the CR

LM2015055, research and development project

Name: Centrum pro systémovou biologii (Acronym: C4SYS)

Investor: Ministry of Education, Youth and Sports of the CR

LM2015085, research and development project

Name: CERIT Scientific Cloud (Acronym: CERIT-SC)

Investor: Ministry of Education, Youth and Sports of the CR, CERIT Scientific Cloud

Citovat

CHRÁST, Lukáš, K. TRATSIAK, Joan PLANAS IGLESIAS, Lukáš DANIEL, T. PRUDNIKOVA, Jan BREZOVSKÝ, David BEDNÁŘ, I.K. SMATANOVA, Radka CHALOUPKOVÁ and Jiří DAMBORSKÝ. Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17. Microorganisms. Basel: MDPI, 2019, vol. 7, No 11, p. 1-20. ISSN 2076-2607. Available from: https://dx.doi.org/10.3390/microorganisms7110498.

@article{1640679,
   author = {Chrást, Lukáš and Tratsiak, K. and Planas Iglesias, Joan and Daniel, Lukáš and Prudnikova, T. and Brezovský, Jan and Bednář, David and Smatanova, I.K. and Chaloupková, Radka and Damborský, Jiří},
   article_location = {Basel},
   article_number = {11},
   doi = {http://dx.doi.org/10.3390/microorganisms7110498},
   keywords = {haloalkane dehalogenase; thermostability; psychrophile; access tunnel; dimer; catalytic pentad; enantiselectivity},
   language = {eng},
   issn = {2076-2607},
   journal = {Microorganisms},
   title = {Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17},
   url = {https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6920932/},
   volume = {7},
   year = {2019}
}

TY  - JOUR
ID  - 1640679
AU  - Chrást, Lukáš - Tratsiak, K. - Planas Iglesias, Joan - Daniel, Lukáš - Prudnikova, T. - Brezovský, Jan - Bednář, David - Smatanova, I.K. - Chaloupková, Radka - Damborský, Jiří
PY  - 2019
TI  - Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17
JF  - Microorganisms
VL  - 7
IS  - 11
SP  - 1-20
EP  - 1-20
PB  - MDPI
SN  - 20762607
KW  - haloalkane dehalogenase
KW  - thermostability
KW  - psychrophile
KW  - access tunnel
KW  - dimer
KW  - catalytic pentad
KW  - enantiselectivity
UR  - https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6920932/
L2  - https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6920932/
N2  - Haloalkane dehalogenases are enzymes with a broad application potential in biocatalysis, bioremediation, biosensing and cell imaging. The new haloalkane dehalogenase DmxA originating from the psychrophilic bacterium Marinobacter sp. ELB17 surprisingly possesses the highest thermal stability (apparent melting temperature T-m,T-app = 65.9 degrees C) of all biochemically characterized wild type haloalkane dehalogenases belonging to subfamily II. The enzyme was successfully expressed and its crystal structure was solved at 1.45 angstrom resolution. DmxA structure contains several features distinct from known members of haloalkane dehalogenase family: (i) a unique composition of catalytic residues; (ii) a dimeric state mediated by a disulfide bridge; and (iii) narrow tunnels connecting the enzyme active site with the surrounding solvent. The importance of narrow tunnels in such paradoxically high stability of DmxA enzyme was confirmed by computational protein design and mutagenesis experiments.
ER  -

CHRÁST, Lukáš, K. TRATSIAK, Joan PLANAS IGLESIAS, Lukáš DANIEL, T. PRUDNIKOVA, Jan BREZOVSKÝ, David BEDNÁŘ, I.K. SMATANOVA, Radka CHALOUPKOVÁ and Jiří DAMBORSKÝ. Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17. \textit{Microorganisms}. Basel: MDPI, 2019, vol.~7, No~11, p.~1-20. ISSN~2076-2607. Available from: https://dx.doi.org/10.3390/microorganisms7110498.

Detailed Information on Publication Record