6IHS

Crystal structure of bacterial serine phosphatase with His-tag mutation

6IHS の概要

• エントリーDOI: 10.2210/pdb6ihs/pdb
• 分子名称: Phosphorylated protein phosphatase, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: bacteria, phosphatase, metal binding, hydrolase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30276.92

構造登録者

Yang, C.-G.,yang, T. (登録日: 2018-10-02, 公開日: 2019-08-07, 最終更新日: 2023-11-22)

主引用文献

Yang, T.,Liu, T.,Gan, J.,Yu, K.,Chen, K.,Xue, W.,Lan, L.,Yang, S.,Yang, C.G.
Structural Insight into the Mechanism of Staphylococcus aureus Stp1 Phosphatase.
Acs Infect Dis., 5:841-850, 2019

PubMed Abstract: Staphylococcus aureus Stp1, which belongs to the bacterial metal-dependent protein phosphatase (PPM) family, is a promising candidate for antivirulence targeting. How Stp1 recognizes the phosphorylated peptide remains unclear, however. In order to investigate the recognition mechanism of Stp1 in depth, we have determined a series of crystal structures of S. aureus Stp1 in different states and the structural complex of Stp1 bound with a phosphorylated peptide His12. Different phosphorylated peptides, including MgrA- and GraR-derived phosphopeptides, are substrates of Stp1, which supports the function of Stp1 as a selective Ser/Thr phosphatase. In addition, interestingly, the crystal structures of R161-Stp1 variants combined with the biochemical activity validations have uncovered that R161 residue plays a key role to control the conformation switches of the flap domain in order to facilitate substrate binding and the dephosphorylation process. Our findings provide crucial structural insight into the molecular mechanism of S. aureus Stp1 phosphatase and reveal the phosphorylated peptides for biochemistry study and inhibitor screening of Stp1.

PubMed: 30868877
DOI: 10.1021/acsinfecdis.8b00316

実験手法

X-RAY DIFFRACTION (1.4 Å)