Crystallization and Crystallographic Analysis of the Rhodococcus rhodochrous NCIMB 13064 Mutant DhaA31 and its Complex with 1,2,3-Trichloropropane

Authors

Lahoda, M., Chaloupková, R., Stsiapanava, A., Damborský, J., Kutá Smatanová, I.

Source

Acta Crystallographica 67

Abstract

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.

Source

Lahoda, M., Chaloupková, R., Stsiapanava, A., Damborský, J., Kutá Smatanová, I.: Crystallization and Crystallographic Analysis of the Rhodococcus rhodochrous NCIMB 13064 Mutant DhaA31 and its Complex with 1,2,3-Trichloropropane, Acta Crystallographica , 67, 397-400, 2011.
[BibTeX] [PDF]


sign in

E-mail:
Password:   

Create new user account

Forgot your password? Please contact us at caver@caver.cz.

HANDS-ON COMPUTATIONAL ENZYME DESIGN COURSE

user statistics

1219 citations
6405 registered users
112037x CAVER downloaded

news

CAVER was cited in NATURE Communications paper entitled Molecular mechanism underlying regulation of...

Read more

June 22, 2023

CAVER was recently cited by the NATURE publication entitled Structural basis of the binding of DNP...

Read more

May 14, 2023

CAVER was recently cited in Nature in paper In situ architecture of the ER–mitochondria encounter...

Read more


other tools

acknowledgement