ArticleNature microbiology2018
Structural insight into the assembly of the type II secretion system pilotin-secretin complex from enterotoxigenic Escherichia coli.
Article in Nature microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Structural insights into the secretin complex of a type IVb pilus system.Nature communications · 2025Article
- pTripleTREP - A vector for tightly controlled expression and purification of virulence factors in Staphylococcus aureus.Microbial cell factories · 2025Article
- Insights into dynamics and gating properties of T2SS secretins.Science advances · 2023Article
- Assembly mechanism of a Tad secretion system secretin-pilotin complex.Nature communications · 2023Article
- Membrane translocation process revealed by in situ structures of type II secretion system secretins.Nature communications · 2023Article
- Review
- Integrative structural analysis of the type III secretion system needle complex from Shigella flexneri.Protein science : a publication of the Protein Society · 2023Article
- Article
- Analysis of diverse eukaryotes suggests the existence of an ancestral mitochondrial apparatus derived from the bacterial type II secretion system.Nature communications · 2021Article
- CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae.Nature communications · 2020Article
- Bacterial secretins: Mechanisms of assembly and membrane targeting.Protein science : a publication of the Protein Society · 2020Review
- In vivo structure of the Legionella type II secretion system by electron cryotomography.Nature microbiology · 2019Article
- Core architecture of a bacterial type II secretion system.Nature communications · 2019Article
- Structure and assembly of pilotin-dependent and -independent secretins of the type II secretion system.PLoS pathogens · 2019Article
- The Dynamic Structures of the Type IV Pilus.Microbiology spectrum · 2019Review
- Architecture, Function, and Substrates of the Type II Secretion System.EcoSal Plus · 2019Review
- Bacterial type III secretion systems: a complex device for the delivery of bacterial effector proteins into eukaryotic host cells.FEMS microbiology letters · 2018Review
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Secretin is a large outer-membrane channel found in secretion systems of Gram-negative bacteria, facilitating the last step for transfer of proteins into the extracellular environment. In the type II secretion system, a lipoprotein called pilotin is essential to bind and target its corresponding secretin to the outer membrane. However, there is only limited structural information available about the interaction and assembly of the pilotin-secretin complex. Here we report the first near-atomic-resolution structure of a full-length Vibrio-type pilotin-secretin (AspS-GspD) complex from enterotoxigenic Escherichia coli by cryo-electron microscopy, which reveals the detailed assembly mode of the full-length pilotin-secretin complex. The AspS subunits attach to the secretin channel surface with a 15:15 stoichiometric ratio to GspD subunits, and insert their amino terminus into the outer membrane. The AspS subunits interact with all three secondary structural elements of the S domain of GspD, including strong interaction with the carboxy-terminal α-helix and weak interactions with another two elements, an α-helix and a loop. These structural and biochemical details provide a deeper insight to pilotin-secretin interaction and their assembly mode.
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