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首页> 外文期刊>Molecular cell >Crystal structure of the PP2A phosphatase activator: Implications for its PP2A-specific PPlase activity
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Crystal structure of the PP2A phosphatase activator: Implications for its PP2A-specific PPlase activity

机译：PP2A磷酸酶激活剂的晶体结构：对PP2A特异性PPlase活性的影响

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摘要

PTPA, an essential and specific activator of protein phosphatase 2A (PP2A), functions as a peptidyl prolyl isomerase (PPlase). We present here the crystal structures of human PTPA and of the two yeast orthologs (Ypa1 and Ypa2), revealing an all alpha-helical protein fold that is radically different from other PPlases. The protein is organized into two domains separated by a groove lined by highly conserved residues. To understand the molecular mechanism of PTPA activity, Ypa1 was cocrystallized with a proline-containing PPIase peptide substrate. In the complex, the peptide binds at the interface of a peptide-induced dimer interface. Conserved residues of the interdomain groove contribute to the peptide binding site and dimer interface. Structure-guided mutational studies showed that in vivo PTPA activity is influenced by mutations on the surface of the peptide binding pocket, the same mutations that also influenced the in vitro activation of PP2Ai and PPIase activity.
机译：PTPA是蛋白质磷酸酶2A（PP2A）的必需和特异性激活剂，可作为肽基脯氨酰异构酶（PPlase）。我们在这里介绍人PTPA和两个酵母直系同源物（Ypa1和Ypa2）的晶体结构，揭示了与其他PPlases根本不同的所有α-螺旋蛋白折叠。蛋白质被组织成两个结构域，两个结构域被高保守性残基衬里的凹槽隔开。为了了解PTPA活性的分子机制，Ypa1与含有脯氨酸的PPIase肽底物共结晶。在复合物中，肽结合在肽诱导的二聚体界面的界面上。域间沟的保守残基有助于肽结合位点和二聚体界面。结构指导的突变研究表明，体内PTPA活性受肽结合袋表面突变的影响，这些突变也影响了PP2Ai和PPIase活性的体外活化。

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