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'''L-2-HALOACID DEHALOGENASE''' | '''L-2-HALOACID DEHALOGENASE''' | ||
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==Reference== | ==Reference== | ||
Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold., Hisano T, Hata Y, Fujii T, Liu JQ, Kurihara T, Esaki N, Soda K, J Biol Chem. 1996 Aug 23;271(34):20322-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8702766 8702766] | Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold., Hisano T, Hata Y, Fujii T, Liu JQ, Kurihara T, Esaki N, Soda K, J Biol Chem. 1996 Aug 23;271(34):20322-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8702766 8702766] | ||
[[Category: Pseudomonas]] | [[Category: Pseudomonas]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Liu, J Q.]] | [[Category: Liu, J Q.]] | ||
[[Category: Soda, K.]] | [[Category: Soda, K.]] | ||
[[Category: | [[Category: Dehalogenase]] | ||
[[Category: | [[Category: Hydrolase]] | ||
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Revision as of 21:56, 2 May 2008
L-2-HALOACID DEHALOGENASE
OverviewOverview
L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic acids. The crystal structure of the homodimeric enzyme from Pseudomonas sp. YL has been determined by a multiple isomorphous replacement method and refined at 2.5 A resolution to a crystallographic R-factor of 19.5%. The subunit consists of two structurally distinct domains: the core domain and the subdomain. The core domain has an alpha/beta structure formed by a six-stranded parallel beta-sheet flanked by five alpha-helices. The subdomain inserted into the core domain has a four helix bundle structure providing the greater part of the interface for dimer formation. There is an active site cavity between the domains. An experimentally identified nucleophilic residue, Asp-10, is located on a loop following the amino-terminal beta-strand in the core domain, and other functional residues, Thr-14, Arg-41, Ser-118, Lys-151, Tyr-157, Ser-175, Asn-177, and Asp-180, detected by a site-directed mutagenesis experiment, are arranged around the nucleophile in the active site. Although the enzyme is an alpha/beta-type hydrolase, it does not belong to the alpha/beta hydrolase fold family, from the viewpoint of the topological feature and the position of the nucleophile.
About this StructureAbout this Structure
1JUD is a Single protein structure of sequence from Pseudomonas. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold., Hisano T, Hata Y, Fujii T, Liu JQ, Kurihara T, Esaki N, Soda K, J Biol Chem. 1996 Aug 23;271(34):20322-30. PMID:8702766 Page seeded by OCA on Fri May 2 21:56:10 2008