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- W3112562425 abstract "Abstract IpaH enzymes are bacterial E3 ligases targeting host proteins for ubiquitylation. Two autoinhibition modes of IpaH enzymes have been proposed based on the relative positioning of the Leucine-rich repeat domain (LRR) with respect to the NEL domain. In mode 1, substrate-binding competitively displaces the interactions between theLRR and NEL to relieve autoinhibition. However, the molecular basis for mode 2 is unclear. Here, we present the crystal structures of Shigella IpaH9.8 and the LRR of IpaH9.8 in complex with the substrate of human guanylate-binding protein 1 (hGBP1). A hydrophobic cluster in the C-terminus of IpaH9.8 LRR forms a hydrophobic pocket involved in binding the NEL domain, and the binding is important for IpaH9.8 autoinhibition. Substrate-binding destabilizes the hydrophobic cluster by inducing conformational changes of IpaH9.8 LRR . Arg166 and Phe187 in IpaH9.8 LRR function as sensors for substrate-binding. Collectively, our findings provide insights into the molecular mechanisms for the actication of IpaH9.8 in autoinhibition mode 2." @default.
- W3112562425 created "2020-12-21" @default.
- W3112562425 creator A5040047154 @default.
- W3112562425 creator A5061800156 @default.
- W3112562425 creator A5079346471 @default.
- W3112562425 date "2020-12-10" @default.
- W3112562425 modified "2023-09-27" @default.
- W3112562425 title "Substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase IpaH9.8" @default.
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- W3112562425 doi "https://doi.org/10.1038/s42003-020-01492-1" @default.
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- W3112562425 hasPublicationYear "2020" @default.
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