Enzyme-substrate interactions revealed by the crystal structures of the archaeal Sulfolobus PTP-fold phosphatase and its phosphopeptide complexes

Hsing Mao Chu, Andrew H.J. Wang

研究成果: 雜誌貢獻文章同行評審

19 引文 斯高帕斯(Scopus)

摘要

The P-loop-containing protein phosphatases are important regulators in signal transduction. These enzymes have structural and functional similarity with a conserved sequence of Dx(25-41) HCsxGxxR(T/S) essential for catalysis. The singular protein tyrosine phosphatase (PTP) from archaeal Sulfolobus solfataricus is one of the smallest known PTPs with extreme thermostability. Here, we report the crystal structure of this phosphatase and its complexes with two tyrosyl phosphopeptides A-(p)Y-R and N-K-(p)Y-G-N. The structure suggests the minimal structural motif of the PTP family, having two variable sequences inserted between the β2-β3 and β3-β4 strands, respectively. The phosphate of both phosphopeptide substrates is bound to the P-loop through several hydrogen bonds. Comparison of several phosphatase-substrate complexes revealed that GM135 on the Q-loop has different modes of recognition toward phosphopeptides. The substrate specificity of SsoPTP is primarily localized at the phosphotyrosine, suggesting that this phosphatase may be a prototypical PTP.

原文英語
頁(從 - 到)996-1003
頁數8
期刊Proteins: Structure, Function and Genetics
66
發行號4
DOIs
出版狀態已發佈 - 3月 2007
對外發佈

ASJC Scopus subject areas

  • 結構生物學
  • 生物化學
  • 分子生物學

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