5MXP

Haloalkane dehalogenase DmxA from Marinobacter sp. ELB17 possessing a unique catalytic residue

Summary for 5MXP

• Entry DOI: 10.2210/pdb5mxp/pdb
• Descriptor: Alpha/beta hydrolase, ACETATE ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: hydrolase, thermostable enzyme, disulfide bridge, unique catalytic residue
• Biological source: Marinobacter sp. ELB17
• Total number of polymer chains: 2
• Total formula weight: 70206.52

Authors

Tratsiak, K.,Rezacova, P.,Prudnikova, T. (deposition date: 2017-01-24, release date: 2018-07-25, Last modification date: 2024-01-17)

Primary citation

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

PubMed 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 sp. ELB17 surprisingly possesses the highest thermal stability (apparent melting temperature = 65.9 °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 Å 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.

PubMed: 31661858
DOI: 10.3390/microorganisms7110498

Experimental method

X-RAY DIFFRACTION (1.45 Å)