Crystal structure of the probable haloacid dehalogenase PH0459 from Pyrococcus horikoshii OT3

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 Å crystal structure of PH0459 (PDB ID: 1X42) determined by the multiwavelength anomalous dispersion method. The core domain has an α/...

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Bibliographic Details
Published in:Protein science 2006-02, Vol.15 (2), p.373-377
Main Authors: Arai, Ryoichi, Kukimoto‐Niino, Mutsuko, Kuroishi, Chizu, Bessho, Yoshitaka, Shirouzu, Mikako, Yokoyama, Shigeyuki
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Binding Sites
Crystallization
Crystallography, X-Ray
detoxification
Dimerization
Disulfides - chemistry
HAD superfamily
haloacid dehalogenase
hydrolase
Hydrolases - chemistry
Hydrolases - genetics
hyperthermophilic archaeon
intracellular disulfide bond
Models, Molecular
Molecular Sequence Data
Protein Conformation
Protein Structure Report
Pseudomonas
Pseudomonas - chemistry
Pyrococcus horikoshii
Pyrococcus horikoshii - chemistry
Pyrococcus horikoshii - genetics
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - isolation & purification
Sequence Homology, Amino Acid
structural genomics
Xanthobacter - chemistry
Xanthobacter autotrophicus
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Summary: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 Å crystal structure of PH0459 (PDB ID: 1X42) determined by the multiwavelength anomalous dispersion method. The core domain has an α/β structure formed by a six‐stranded parallel β‐sheet flanked by six α‐helices and three 310‐helices. One disulfide bond, Cys186–Cys212, forms a bridge between an α‐helix and a 310‐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.
ISSN:0961-8368
1469-896X
DOI:10.1110/ps.051922406