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Atomic resolution studies of haloalkane dehalogenases DhaA04, DhaA14 and DhaA15 with engineered access tunnels
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SYSNO ASEP 0346383 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Atomic resolution studies of haloalkane dehalogenases DhaA04, DhaA14 and DhaA15 with engineered access tunnels Author(s) Stsiapanava, A. (CZ)
Dohnálek, Jan (UMCH-V) RID
Gavira, J. A. (ES)
Kutý, Michal (UEK-B)
Koudeláková, T. (CZ)
Damborský, J. (CZ)
Kutá-Smatanová, Ivana (UEK-B) RIDSource Title Acta Crystallographica Section D-Biological Crystallography. - : WILEY-BLACKWELL - ISSN 0907-4449
Roč. 66, č. 9 (2010), s. 962-969Number of pages 8 s. Language eng - English Country DK - Denmark Keywords haloalkane dehalogenase DhaA ; Rhodococcus rhodochrous ; mutagenesis Subject RIV CE - Biochemistry R&D Projects GA310/09/1407 GA ČR - Czech Science Foundation (CSF) LC06010 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) CEZ AV0Z40500505 - UMCH-V (2005-2011) AV0Z60870520 - UEK-B (2005-2011) UT WOS 000281635500002 DOI 10.1107/S0907444910027101 Annotation Mutagenesis focused on the access tunnels of DhaA produced protein variants with significantly improved activity towards TCP. Three mutants of DhaA named DhaA04 (C176Y), DhaA14 (I135F) and DhaA15 (C176Y + I135F) were constructed in order to study the functional relevance of the enzyme tunnels The crystal structures of DhaA04, DhaA14 and DhaA15 with ligands present in the active site were solved and refined using diffraction data to 1.23, 0.95 and 1.22 Å, resolution, respectively. Structural comparisons of the wild type and the three mutants suggest that the tunnels play a key role in the processes of ligand exchange between the buried active site and the surrounding solvent. Workplace Institute of Macromolecular Chemistry Contact Eva Čechová, cechova@imc.cas.cz ; Tel.: 296 809 358 Year of Publishing 2011
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