1aq6
STRUCTURE OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER AUTOTROPHICUS
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OverviewOverview
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.
About this StructureAbout this Structure
1AQ6 is a Single protein structure of sequence from Xanthobacter autotrophicus with FMT as ligand. Active as (S)-2-haloacid dehalogenase, with EC number 3.8.1.2 Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate., Ridder IS, Rozeboom HJ, Kalk KH, Janssen DB, Dijkstra BW, J Biol Chem. 1997 Dec 26;272(52):33015-22. PMID:9407083
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