ArticleNature communications2019
Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Evolution of N-terminal mechanical lability as a determinant for Type III secretion.Protein science : a publication of the Protein Society · 2026Article
- Type III secretion system chaperones: a helping hand for secretion.Microbiology (Reading, England) · 2026Review
- Structure of the proton-powered secretion motor at the heart of the bacterial flagellum.bioRxiv : the preprint server for biology · 2026Article
- Structural and Biophysical Characterization of the Yersinia Type Three Secretion System ATPase YscN.Proteins · 2026Article
- Article
- Uncoupling substrate delivery from export gate activation reveals distinct roles of the flagellar ATPase complex.Frontiers in microbiology · 2026Article
- A Type III secretion system effector evolved to be mechanically labile and initiate unfolding from the N-terminus.bioRxiv : the preprint server for biology · 2026Article
- Cyclic-di-GMP controls Type III effector export and symptom development in Pseudomonas syringae infections via the export ATPase HrcN.PLoS pathogens · 2025Article
- Functional and structural characterization of FProtein science : a publication of the Protein Society · 2025Article
- The predicted sorting platform dynamically associates with the type III secretion system from Xanthomonas euvesicatoria in response to the external pH.BMC microbiology · 2025Article
- Dimeric assembly of FScience advances · 2025Article
- The promiscuous biotin ligase TurboID reveals the proxisome of the T3SS chaperone IpgC inmSphere · 2024Article
- Virulence-associated type III secretion systems in Gram-negative bacteria.Microbiology (Reading, England) · 2023Review
- Primary architecture and energy requirements of Type III and Type IV secretion systems.Frontiers in cellular and infection microbiology · 2023Review
- Differential regulation ofFrontiers in cellular and infection microbiology · 2023Article
- Assembly and architecture of the type III secretion sorting platform.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Cryo-EM of the injectisome and type III secretion systems.Current opinion in structural biology · 2022Review
- Enhanced protein translocation to mammalian cells by expression of EtgA transglycosylase in a synthetic injector E. coli strain.Microbial cell factories · 2022Article
- Orf1B controls secretion of T3SS proteins and contributes to Edwardsiella piscicida adhesion to epithelial cells.Veterinary research · 2022Article
- N-terminal signal peptides facilitate the engineering of PVC complex as a potent protein delivery system.Science advances · 2022Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many Gram-negative bacteria, including causative agents of dysentery, plague, and typhoid fever, rely on a type III secretion system - a multi-membrane spanning syringe-like apparatus - for their pathogenicity. The cytosolic ATPase complex of this injectisome is proposed to play an important role in energizing secretion events and substrate recognition. We present the 3.3 Å resolution cryo-EM structure of the enteropathogenic Escherichia coli ATPase EscN in complex with its central stalk EscO. The structure shows an asymmetric pore with different functional states captured in its six catalytic sites, details directly supporting a rotary catalytic mechanism analogous to that of the heterohexameric F
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