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 Cited by 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: 9407083DOI: 10.1074/jbc.272.52.33015 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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