2QVB

Crystal Structure of Haloalkane Dehalogenase Rv2579 from Mycobacterium tuberculosis

Summary for 2QVB

• Entry DOI: 10.2210/pdb2qvb/pdb
• Descriptor: Haloalkane dehalogenase 3, CHLORIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: rv2579, haloalkane dehalogenase, alpha-beta hydrolase protein, tb structural genomics consortium, tbsgc, hydrolase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 2
• Total formula weight: 67060.36

Authors

Mazumdar, P.A.,Hulecki, J.,Cherney, M.M.,Garen, C.R.,James, M.N.G.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2007-08-08, release date: 2008-02-12, Last modification date: 2023-08-30)

Primary citation

Mazumdar, P.A.,Hulecki, J.C.,Cherney, M.M.,Garen, C.R.,James, M.N.
X-ray crystal structure of Mycobacterium tuberculosis haloalkane dehalogenase Rv2579.
Biochim.Biophys.Acta, 1784:351-362, 2008

PubMed Abstract: Haloalkane dehalogenases are enzymes well known to be important in bioremediation; the organisms from which they are produced are able to clean up toxic organohalides from polluted environments. However, besides being found in such contaminated environments, these enzymes have also been found in root or tissue-colonizing bacterial species. The haloalkane dehalogenase Rv2579 from Mycobacterium tuberculosis H37Rv has been cloned, expressed, purified and its crystal structure determined at high resolution (1.2A). In addition, the crystal structure of the enzyme has been determined in complex with the product from the reaction with 1,3-dibromopropane, i.e. 1,3-propanediol and in complex with the classical substrate of haloalkane dehalogenases, 1,2-dichloroethane. The enzyme is a two-domain protein having a catalytic domain of an alpha/beta hydrolase fold and a cap domain. The active site residues and the halide-stabilizing residues have been identified as Asp109, Glu133, His273, Asn39 and Trp110. Its overall structure is similar to those of other known haloalkane dehalogenases. Its mechanism of action involves an SN2 nucleophilic displacement.

PubMed: 18062934
DOI: 10.1016/j.bbapap.2007.10.014

Experimental method

X-RAY DIFFRACTION (1.19 Å)