Number of the records: 1
Crystallization and Crystallographic Analysis of a Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant with an Eliminated Halide-Binding Site
- 1.
SYSNO ASEP 0508541 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Crystallization and Crystallographic Analysis of a Bradyrhizobium Elkanii USDA94 Haloalkane Dehalogenase Variant with an Eliminated Halide-Binding Site Author(s) Prudnikova, Tatyana (MBU-M)
Kascaková, B. (CZ)
Mesters, J. R. (DE)
Grinkevich, P. (CZ)
Havlíčková, P. (CZ)
Mazur, Andrii (MBU-M)
Shaposhnikova, Anastasiia (MBU-M)
Chaloupková, R. (CZ)
Dambrovský, J. (CZ)
Kutý, Michal (MBU-M) ORCID
Kutá Smatanová, Ivana (MBU-M) ORCIDArticle number 375 Source Title Crystals. - : MDPI - ISSN 2073-4352
Roč. 9, č. 7 (2019)Number of pages 12 s. Language eng - English Country CH - Switzerland Keywords Haloalkane dehalogenase ; halide-binding site ; random microseeding Subject RIV CE - Biochemistry 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. Method of publishing Open access Institutional support MBU-M - RVO:61388971 UT WOS 000482052800024 EID SCOPUS 85071098152 DOI 10.3390/cryst9070375 Annotation Haloalkane dehalogenases are a very important class of microbial enzymes for environmental detoxification of halogenated pollutants, for biocatalysis, biosensing and molecular tagging. The double mutant (Ile44Leu + Gln102His) of the haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94 (DbeA Delta Cl) was constructed to study the role of the second halide-binding site previously discovered in the wild-type structure. The variant is less active, less stable in the presence of chloride ions and exhibits significantly altered substrate specificity when compared with the DbeAwt. DbeA Delta Cl was crystallized using the sitting-drop vapour-diffusion procedure with further optimization by the random microseeding technique. The crystal structure of the DbeA Delta Cl has been determined and refined to the 1.4 angstrom resolution. The DbeA Delta Cl crystals belong to monoclinic space group C121. The DbeA Delta Cl molecular structure was characterized and compared with five known haloalkane dehalogenases selected from the Protein Data Bank. 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/2073-4352/9/7/375
Number of the records: 1