1X42

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

1X42 の概要

• エントリーDOI: 10.2210/pdb1x42/pdb
• 分子名称: hypothetical protein PH0459 (2 entities in total)
• 機能のキーワード: haloacid dehalogenase, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, hydrolase
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27092.98

構造登録者

Arai, R.,Kukimoto-Niino, M.,Sugahara, M.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2005-05-12, 公開日: 2005-11-12, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2 Å)