3WJ8

Crystal Structure of DL-2-haloacid dehalogenase mutant with 2-bromo-2-methylpropionate

Summary for 3WJ8

• Entry DOI: 10.2210/pdb3wj8/pdb
• Related: 4N2X
• Descriptor: DL-2-haloacid dehalogenase, 2-bromo-2-methylpropanoic acid, GLYCEROL, ... (4 entities in total)
• Functional Keywords: dehalogenases, hydrolase
• Biological source: Methylobacterium
• Total number of polymer chains: 6
• Total formula weight: 206112.10

Authors

Siwek, A.,Omi, R.,Hirotsu, K.,Jitsumori, K.,Esaki, N.,Kurihara, T.,Paneth, P. (deposition date: 2013-10-07, release date: 2013-11-27, Last modification date: 2024-03-20)

Primary citation

Siwek, A.,Omi, R.,Hirotsu, K.,Jitsumori, K.,Esaki, N.,Kurihara, T.,Paneth, P.
Binding modes of DL-2-haloacid dehalogenase revealed by crystallography, modeling and isotope effects studies.
Arch.Biochem.Biophys., 540:26-32, 2013

PubMed Abstract: Several pathways of biotic dechlorination can be found in enzymes, each characterized by different chlorine isotopic fractionation, which can thus serve as a signature of a particular mechanism. Unlike other dehalogenases, DL-2-haloacid dehalogenase, DL-DEX, converts both enantiomers of the substrate. Chlorine isotope effects for this enzyme are larger than in the case of other dehalogenases. Recently, the 3D structure of this enzyme became available and enabled us to model these isotope effects and seek their origin. We show that the elevated values of the chlorine kinetic isotope effects originate in part in the processes of binding and migration within the enzyme active site that precede the dehalogenation step.

PubMed: 24071515
DOI: 10.1016/j.abb.2013.09.012

Experimental method

X-RAY DIFFRACTION (2.7 Å)