1X42

Crystal structure of a haloacid dehalogenase family protein (PH0459) from Pyrococcus horikoshii OT3

Summary for 1X42

• Entry DOI: 10.2210/pdb1x42/pdb
• Descriptor: hypothetical protein PH0459 (2 entities in total)
• Functional Keywords: haloacid dehalogenase, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, hydrolase
• Biological source: Pyrococcus horikoshii
• Total number of polymer chains: 1
• Total formula weight: 27092.98

Authors

Arai, R.,Kukimoto-Niino, M.,Sugahara, M.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2005-05-12, release date: 2005-11-12, Last modification date: 2024-10-23)

Primary citation

Arai, R.,Kukimoto-Niino, M.,Kuroishi, C.,Bessho, Y.,Shirouzu, M.,Yokoyama, S.
Crystal structure of the probable haloacid dehalogenase PH0459 from Pyrococcus horikoshii OT3
Protein Sci., 15:373-377, 2006

PubMed 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.

PubMed: 16385007
DOI: 10.1110/ps.051922406

Experimental method

X-RAY DIFFRACTION (2 Å)