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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F19%3A43899727" target="_blank" >RIV/60076658:12310/19:43899727 - isvavai.cz</a>

Alternative codes found

RIV/61388971:_____/19:00520840 RIV/61388963:_____/19:00511267 RIV/00216224:14310/19:00108215 RIV/00159816:_____/19:00072470

Result on the web

<a href="https://www.mdpi.com/2076-2607/7/11/498/htm" target="_blank" >https://www.mdpi.com/2076-2607/7/11/498/htm</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3390/microorganisms7110498" target="_blank" >10.3390/microorganisms7110498</a>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10606 - Microbiology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2019

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Microorganisms

ISSN

2076-2607

e-ISSN

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Volume of the periodical

7

Issue of the periodical within the volume

11

Country of publishing house

CH - SWITZERLAND

Number of pages

20

Pages from-to

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UT code for WoS article

000502273600021

EID of the result in the Scopus database

2-s2.0-85074389188