Structure Report for: 5MXP

Chrast, L., Tratsiak, K., Daniel, L., Prudnikova, T., Brezovsky, J., Smatanova, I.K., Chaloupkova, R., Damborsky, J.Structural basis of paradoxically high thermostability of dehalogenase from psychrophilic bacterium

Title: Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic Bacterium Marinobacter sp. ELB17
Chrast L, Tratsiak K, Planas-Iglesias J, Daniel L, Prudnikova T, Brezovsky J, Bednar D, Kuta Smatanova I, Chaloupkova R, Damborsky J
Ref: Microorganisms, 7:, 2019 : PubMed
Abstract


ESTHER: Chrast_2019_Microorganisms_7_
PubMedSearch: Chrast 2019 Microorganisms 7
PubMedID: 31661858
Gene_locus related to this paper: 9alte-a3jb27

Abstract

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 Tm,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 A 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.



        

Title: Crystallographic analysis of new psychrophilic haloalkane dehalogenases: DpcA from Psychrobacter cryohalolentis K5 and DmxA from Marinobacter sp. ELB17
Tratsiak K, Degtjarik O, Drienovska I, Chrast L, Rezacova P, Kuty M, Chaloupkova R, Damborsky J, Kuta Smatanova I
Ref: Acta Crystallographica Sect F Struct Biol Cryst Commun, 69:683, 2013 : PubMed
Abstract


ESTHER: Tratsiak_2013_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_69_683
PubMedSearch: Tratsiak 2013 Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun 69 683
PubMedID: 23722854
Gene_locus related to this paper: 9alte-a3jb27, psyck-q1qbb9

Abstract

Haloalkane dehalogenases are hydrolytic enzymes with a broad range of potential practical applications such as biodegradation, biosensing, biocatalysis and cellular imaging. Two newly isolated psychrophilic haloalkane dehalogenases exhibiting interesting catalytic properties, DpcA from Psychrobacter cryohalolentis K5 and DmxA from Marinobacter sp. ELB17, were purified and used for crystallization experiments. After the optimization of crystallization conditions, crystals of diffraction quality were obtained. Diffraction data sets were collected for native enzymes and complexes with selected ligands such as 1-bromohexane and 1,2-dichloroethane to resolutions ranging from 1.05 to 2.49 A.