1aq6
From Proteopedia
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[[Image:1aq6.jpg|left|200px]] | [[Image:1aq6.jpg|left|200px]] | ||
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'''STRUCTURE OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER AUTOTROPHICUS''' | '''STRUCTURE OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER AUTOTROPHICUS''' | ||
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==Reference== | ==Reference== | ||
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:[http://www.ncbi.nlm.nih.gov/pubmed/9407083 9407083] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9407083 9407083] | ||
- | [[Category: (S)-2-haloacid dehalogenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xanthobacter autotrophicus]] | [[Category: Xanthobacter autotrophicus]] | ||
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[[Category: Ridder, I S.]] | [[Category: Ridder, I S.]] | ||
[[Category: Rozeboom, H J.]] | [[Category: Rozeboom, H J.]] | ||
- | [[Category: | + | [[Category: L-2-haloacid dehalogenase]] |
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Revision as of 07:34, 2 May 2008
STRUCTURE OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER AUTOTROPHICUS
Overview
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 Structure
1AQ6 is a Single protein structure of sequence from Xanthobacter autotrophicus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 10:34:38 2008