ArticleCommunications biology2020
Substrate-binding destabilizes the hydrophobic cluster to relieve the autoinhibition of bacterial ubiquitin ligase IpaH9.8.
Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Targeting of ELMO2 by thebioRxiv : the preprint server for biology · 2026Article
- Covalent fragment screening to inhibit the E3 ligase activity of bacterial NEL enzymes SspH1 and SspH2.RSC chemical biology · 2026Article
- Crystal structures reveal nucleotide-induced conformational changes in G motifs and distal regions in human guanylate-binding protein 2.Communications biology · 2025Article
- Lipid-mediated intracellular delivery of recombinant bioPROTACs for the rapid degradation of undruggable proteins.Nature communications · 2024Article
- Ubiquitin-targeted bacterial effectors: rule breakers of the ubiquitin system.The EMBO journal · 2023Review
- Article
- Insights into the GSDMB-mediated cellular lysis and its targeting by IpaH7.8.Nature communications · 2023Article
- The NEL Family of Bacterial E3 Ubiquitin Ligases.International journal of molecular sciences · 2022Review
- Chromosome-encoded IpaH ubiquitin ligases indicate non-human enteroinvasive Escherichia.Scientific reports · 2022Article
- Efficient production of immunologically active Shigella invasion plasmid antigens IpaB and IpaH using a cell-free expression system.Applied microbiology and biotechnology · 2022Article
- Shigella ubiquitin ligase IpaH7.8 targets gasdermin D for degradation to prevent pyroptosis and enable infection.Cell host & microbe · 2021Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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
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