J 2011

Crystallization and Preliminary X-ray Diffraction Analysis of the Wild-Type Haloalkane Dehalogenase DhaA and its Variant DhaA13 Complexed with Different Ligands

STSIAPANAVA, Alena, Radka CHALOUPKOVÁ, Andrea FOŘTOVÁ, J. BRYNDA, M. S. WEISS et. al.

Basic information

Original name

Crystallization and Preliminary X-ray Diffraction Analysis of the Wild-Type Haloalkane Dehalogenase DhaA and its Variant DhaA13 Complexed with Different Ligands

Authors

STSIAPANAVA, Alena (112 Belarus, belonging to the institution), Radka CHALOUPKOVÁ (203 Czech Republic, belonging to the institution), Andrea FOŘTOVÁ (203 Czech Republic, belonging to the institution), J. BRYNDA (203 Czech Republic), M. S. WEISS (203 Czech Republic), Jiří DAMBORSKÝ (203 Czech Republic, guarantor, belonging to the institution) and Ivana KUTÁ-SMATANOVÁ (203 Czech Republic, belonging to the institution)

Edition

Acta Crystallographica F, 2011, 1744-3091

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 0.506

RIV identification code

RIV/00216224:14310/11:00049440

Organization unit

Faculty of Science

DOI

UT WoS

000287030600018

Keywords in English

Crystallization; X-ray Diffraction Analysis; Haloalkane Dehalogenase DhaA

Tags

Změněno: 20/4/2012 10:35, Ing. Andrea Mikešková

Abstract

V originále

Haloalkane dehalogenases make up an important class of hydrolytic enzymes which catalyse the cleavage of carbon-halogen bonds in halogenated aliphatic compounds. There is growing interest in these enzymes owing to their potential use in environmental and industrial applications. The haloalkane dehalogenase DhaA fromRhodococcus rhodochrous NCIMB 13064 can slowly detoxify the industrial pollutant 1,2,3-trichloropropane (TCP). Structural analysis of this enzyme complexed with target ligands was conducted in order to obtain detailed information about the structural limitations of its catalytic properties. In this study, the crystallization and preliminary X-ray analysis of complexes of wild-type DhaA with 2-propanol and with TCP and of complexes of the catalytically inactive variant DhaA13 with the dye coumarin and with TCP are described.

Links

ED0001/01/01, research and development project
Name: CETOCOEN
IAA401630901, research and development project
Name: Evoluce substrátové specifity u enzymů aktivních s xenobiotickými látkami
Investor: Academy of Sciences of the Czech Republic, Evolution of substrate specificity in enzymes acting on xenobiotic compounds
LC06010, research and development project
Name: Centrum biokatalýzy a biotransformací
Investor: Ministry of Education, Youth and Sports of the CR, Center of Biocatalysis and Biotransformation
MSM0021622412, plan (intention)
Name: Interakce mezi chemickými látkami, prostředím a biologickými systémy a jejich důsledky na globální, regionální a lokální úrovni (INCHEMBIOL) (Acronym: INCHEMBIOL)
Investor: Ministry of Education, Youth and Sports of the CR, Interactions among the chemicals, environment and biological systems and their consequences on the global, regional and local scales (INCHEMBIOL)
MSM0021622413, plan (intention)
Name: Proteiny v metabolismu a při interakci organismů s prostředím
Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment