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

Publikace nespadá pod Filozofickou fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.

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CHRÁST Lukáš TRATSIAK K. PLANAS IGLESIAS Joan DANIEL Lukáš PRUDNIKOVA T. BREZOVSKÝ Jan BEDNÁŘ David SMATANOVA I.K. CHALOUPKOVÁ Radka DAMBORSKÝ Jiří

Druh Článek v odborném periodiku
Časopis / Zdroj Microorganisms
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
www https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6920932/
Doi http://dx.doi.org/10.3390/microorganisms7110498
Klíčová slova haloalkane dehalogenase; thermostability; psychrophile; access tunnel; dimer; catalytic pentad; enantiselectivity
Popis 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.
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