Crystal Structure of the Probable Haloacid Dehalogenase Ph0459 from Pyrococcus Horikoshii Ot3.
From: Protein Research Group, Genomic Sciences Center, RIKEN Yokohama Institute, 1-7-22, Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan.
Protein science : a publication of the Protein Society
- Publish Date: Feb 2006
- ISSN: 0961-8368
- Volume: 15
- Issue: 2
- Pages: 373-7
- Medium: Print
- Language: English
- Citation (JAMA): Arai Ryoichi, Kukimoto-Niino Mutsuko, Kuroishi Chizu, et al. Crystal Structure of the Probable Haloacid Dehalogenase Ph0459 from Pyrococcus Horikoshii Ot3.. Protein Sci. Feb 2006;15:373-7
Abstract
PH0459, from the hyperthermophilic archaeon Pyrococcus horikoshii OT3, is a probable haloacid dehalogenase with a molecular mass of 26,725 Da. Here, we report the 2.0 A crystal structure of PH0459 (PDB ID: 1X42) determined by the multiwavelength anomalous dispersion method. The core domain has an alpha/beta structure formed by a six-stranded parallel beta-sheet flanked by six alpha-helices and three 3(10)-helices. One disulfide bond, Cys186-Cys212, forms a bridge between an alpha-helix and a 3(10)-helix, although PH0459 seems to be an intracellular protein. The subdomain inserted into the core domain has a four-helix bundle structure. The crystal packing suggests that PH0459 exists as a monomer. A structural homology search revealed that PH0459 resembles the l-2-haloacid dehalogenases l-DEX YL from Pseudomonas sp. YL and DhlB from Xanthobacter autotrophicus GJ10. A comparison of the active sites suggested that PH0459 probably has haloacid dehalogenase activity, but its substrate specificity may be different. In addition, the disulfide bond in PH0459 probably facilitates the structural stabilization of the neighboring region in the monomeric form, although the corresponding regions in l-DEX YL and DhlB may be stabilized by dimerization. Since heat-stable dehalogenases can be used for the detoxification of halogenated aliphatic compounds, PH0459 will be a useful target for biotechnological research.
Mesh Headings (Keywords): Amino Acid Sequence, Binding Sites, Crystallization, Crystallography, X-Ray, Dimerization, Disulfides, Hydrolases, Models, Molecular, Molecular Sequence Data, Protein Conformation, Pseudomonas, Pyrococcus horikoshii, Recombinant Proteins, Sequence Homology, Amino Acid, Xanthobacter
Check for Full Text / PubMed Unique Identifier (PMID): 16385007
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