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Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17
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SYSNO ASEP 0520840 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17 Author(s) Chrást, L. (CZ)
Tratsiak, K. (CZ)
Planas-Iglesias, J. (CZ)
Daniel, L. (CZ)
Prudnikova, Tatyana (MBU-M)
Brezovský, J. (CZ)
Bednář, D. (CZ)
Kutá Smatanová, Ivana (MBU-M) ORCID
Chaloupková, R. (CZ)
Dambrovský, J. (CZ)Article number 498 Source Title Microorganisms. - : MDPI
Roč. 7, č. 11 (2019)Number of pages 20 s. Language eng - English Country CH - Switzerland Keywords haloalkane dehalogenase ; thermostability ; psychrophile Subject RIV EE - Microbiology, Virology OECD category Biochemistry and molecular biology R&D Projects LM2015055 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Research Infrastructure C4SYS - 90055 - Mikrobiologický ústav AV ČR, v. v. i.
RECETOX II - 90051 - Masarykova univerzita
ELIXIR-CZ - 90047 - Ústav organické chemie a biochemie AV ČR, v. v. i.
CESNET II - 90042 - CESNET - zájmové sdružení právnických osob
CERIT-SC - 90085 - Masarykova univerzitaMethod of publishing Open access Institutional support MBU-M - RVO:61388971 UT WOS 000502273600021 EID SCOPUS 85074389188 DOI 10.3390/microorganisms7110498 Annotation 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. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2020 Electronic address https://www.mdpi.com/2076-2607/7/11/498
Number of the records: 1