Crystallization and crystallographic analysis of the Rhodococcus rhodochrous NCIMB 13064 DhaA mutant DhaA31 and its complex with 1,2,3-trichloropropane
Jazyk angličtina Země Velká Británie, Anglie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
21393851
PubMed Central
PMC3053171
DOI
10.1107/s1744309111001254
PII: S1744309111001254
Knihovny.cz E-zdroje
- MeSH
- bakteriální proteiny chemie genetika metabolismus MeSH
- difrakce rentgenového záření MeSH
- hydrolasy chemie genetika metabolismus MeSH
- krystalizace MeSH
- molekulární sekvence - údaje MeSH
- propan analogy a deriváty chemie metabolismus MeSH
- Rhodococcus enzymologie MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- 1,2,3-trichloropropane MeSH Prohlížeč
- bakteriální proteiny MeSH
- haloalkane dehalogenase MeSH Prohlížeč
- hydrolasy MeSH
- propan MeSH
Haloalkane dehalogenases hydrolyze carbon-halogen bonds in a wide range of halogenated aliphatic compounds. The potential use of haloalkane dehalogenases in bioremediation applications has stimulated intensive investigation of these enzymes and their engineering. The mutant DhaA31 was constructed to degrade the anthropogenic compound 1,2,3-trichloropropane (TCP) using a new strategy. This strategy enhances activity towards TCP by decreasing the accessibility of the active site to water molecules, thereby promoting formation of the activated complex. The structure of DhaA31 will help in understanding the structure-function relationships involved in the improved dehalogenation of TCP. The mutant protein DhaA31 was crystallized by the sitting-drop vapour-diffusion technique and crystals of DhaA31 in complex with TCP were obtained using soaking experiments. Both crystals belonged to the triclinic space group P1. Diffraction data were collected to high resolution: to 1.31 Å for DhaA31 and to 1.26 Å for DhaA31 complexed with TCP.
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