1AQ6

STRUCTURE OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER AUTOTROPHICUS

Summary for 1AQ6

• Entry DOI: 10.2210/pdb1aq6/pdb
• Descriptor: L-2-HALOACID DEHALOGENASE, FORMIC ACID (3 entities in total)
• Functional Keywords: l-2-haloacid dehalogenase, dehalogenase
• Biological source: Xanthobacter autotrophicus
• Total number of polymer chains: 2
• Total formula weight: 55126.82

Authors

Ridder, I.S.,Rozeboom, H.J.,Kalk, K.H.,Dijkstra, B.W. (deposition date: 1997-08-07, release date: 1998-01-28, Last modification date: 2024-02-07)

Primary citation

Ridder, I.S.,Rozeboom, H.J.,Kalk, K.H.,Janssen, D.B.,Dijkstra, B.W.
Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate.
J.Biol.Chem., 272:33015-33022, 1997

PubMed Abstract: The L-2-haloacid dehalogenase from the 1,2-dichloroethane degrading bacterium Xanthobacter autotrophicus GJ10 catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. Its crystal structure was solved by the method of multiple isomorphous replacement with incorporation of anomalous scattering information and solvent flattening, and was refined at 1.95-A resolution to an R factor of 21.3%. The three-dimensional structure is similar to that of the homologous L-2-haloacid dehalogenase from Pseudomonas sp. YL (1), but the X. autotrophicus enzyme has an extra dimerization domain, an active site cavity that is completely shielded from the solvent, and a different orientation of several catalytically important amino acid residues. Moreover, under the conditions used, a formate ion is bound in the active site. The position of this substrate-analogue provides valuable information on the reaction mechanism and explains the limited substrate specificity of the Xanthobacter L-2-haloacid dehalogenase.

PubMed: 9407083
DOI: 10.1074/jbc.272.52.33015

Experimental method

X-RAY DIFFRACTION (1.95 Å)