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首页> 外文期刊>Structure >A Structure-Based Model of Substrate Discrimination by a Noncanonical PDZ Tandem in the Intramembrane-Cleaving Protease RseP
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A Structure-Based Model of Substrate Discrimination by a Noncanonical PDZ Tandem in the Intramembrane-Cleaving Protease RseP

机译：基于结构的非经典PDZ串联在膜内蛋白酶RseP区分的基质的模型。

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During the extracytoplasmic stress response in Escherichia coli, the intramembrane protease RseP cleaves the anti-σ~E protein RseA only after the membrane- anchored protease DegS truncates the periplasmic part of RseA that suppresses the action of RseP. Herewe analyzed the three-dimensional structure of the two tandemly arranged PSD-95/Dlg/ZO-1 (PDZ) domains (PDZ tandem) present in the periplasmic region of RseP and revealed that the two putative ligand-binding grooves constitute a single pocketlike structure that would lie just above the active center sequestrated within the membrane. Complete removal of the PDZ tandem from RseP led to the intramembrane cleavage of RseA without prior truncation by DegS. Furthermore, mutations expected to destabilize the tertiary structure of the PDZ tandem also caused the deregulation of the sequential cleavage. These observations suggest that the PDZ tandem serves as a size-exclusion filter to accommodate the truncated form of RseA into the active center.
机译：在大肠杆菌的胞质外应激反应过程中，仅在膜锚定蛋白酶DegS截短RseA的周质部分以抑制RseP作用后，膜内蛋白酶RseP才切割抗σE蛋白RseA。在此我们分析了RseP周质区域中两个串联排列的PSD-95 / Dlg / ZO-1（PDZ）域（PDZ串联）的三维结构，并揭示了两个推定的配体结合凹槽构成单个袋状该结构恰好位于隔离在膜内的活性中心之上。从RseP中完全去除PDZ串联导致RseA的膜内切割，而没有被DegS事先截断。此外，预期使PDZ串联三级结构不稳定的突变也引起顺序切割的失调。这些观察结果表明，PDZ串联用作大小排阻过滤器，以将截短形式的RseA容纳到活动中心。

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