1UJC

Structure of the protein histidine phosphatase SixA complexed with tungstate

1UJC の概要

• エントリーDOI: 10.2210/pdb1ujc/pdb
• 関連するPDBエントリー: 1UJB
• 分子名称: Phosphohistidine phosphatase sixA, CALCIUM ION, TUNGSTATE(VI)ION, ... (4 entities in total)
• 機能のキーワード: alpha-beta fold, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17506.62

構造登録者

Hamada, K.,Kato, M.,Shimizu, T.,Ihara, K.,Mizuno, T.,Hakoshima, T. (登録日: 2003-07-31, 公開日: 2005-01-25, 最終更新日: 2023-12-27)

主引用文献

Hamada, K.,Kato, M.,Shimizu, T.,Ihara, K.,Mizuno, T.,Hakoshima, T.
Crystal structure of the protein histidine phosphatase SixA in the multistep His-Asp phosphorelay.
Genes Cells, 10:1-11, 2005

PubMed Abstract: The multiple histidine-aspartate phosphorelay system plays a crucial role in cellular adaptation to environments in microorganisms and plants. Like kinase-phosphatase systems in higher eukaryotes, the multiple steps provide additional regulatory checkpoints with phosphatases. The Escherichia coli phosphatase SixA exhibits protein phosphatase activity against the histidine-containing phosphotransfer (HPt) domain located in the C-terminus of the histidine kinase ArcB engaged in anaerobic responses. We have determined the crystal structures of the free and tungstate-bound forms of SixA at 2.06 A and 1.90 A resolution, respectively. The results provide the first three-dimensional view of a bacterial protein histidine phosphatase, revealing a compact alpha/beta architecture related to a family of phosphatases containing the arginine-histidine-glycine (RHG) motif at their active sites. Compared with these RHG phosphatases, SixA lacks an extra alpha-helical subdomain as a lid over the active site, thereby forming a relatively shallow groove important for the accommodation of the HPt domain of ArcB. The tungstate ion, which mimics the substrate phosphate group, is located at the centre of the active site where the active residue, His8, points to the tungsten atom in the mode of in-line nucleophilic attack.

PubMed: 15670209
DOI: 10.1111/j.1365-2443.2005.00817.x

実験手法

X-RAY DIFFRACTION (1.9 Å)