ArticlePLoS pathogens2011
Structural and functional studies on the interaction of GspC and GspD in the type II secretion system.
Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 97 citations in OpenAlex.
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- Structural insights into the Thermus thermophilus type IV pilus machinery assembling two distinct pili.Communications biology · 2026Article
- Electron Cryo-Tomography Reveals thebioRxiv : the preprint server for biology · 2025Article
- The PDZ domain of EpsC is required for extracellular secretion of VesB by the Type II secretion system inJournal of bacteriology · 2025Article
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- Type IV pili ofEcoSal Plus · 2024Review
- PilY1 regulates the dynamic architecture of the type IV pilus machine in Pseudomonas aeruginosa.Nature communications · 2024Article
- Insights into dynamics and gating properties of T2SS secretins.Science advances · 2023Article
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- Comparative Genomics Assisted Functional Characterization ofFrontiers in microbiology · 2022Article
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- Analysis of diverse eukaryotes suggests the existence of an ancestral mitochondrial apparatus derived from the bacterial type II secretion system.Nature communications · 2021Article
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- Secrete or perish: The role of secretion systems inComputational and structural biotechnology journal · 2021Review
- Bacterial secretins: Mechanisms of assembly and membrane targeting.Protein science : a publication of the Protein Society · 2020Review
- Cryo-EM structure of the Shigella type III needle complex.PLoS pathogens · 2020Article
- 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
- Electron Cryotomography of Bacterial Secretion Systems.Microbiology spectrum · 2019Article
- The Dynamic Structures of the Type IV Pilus.Microbiology spectrum · 2019Review
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
Abstract
Type II secretion systems (T2SSs) are critical for secretion of many proteins from Gram-negative bacteria. In the T2SS, the outer membrane secretin GspD forms a multimeric pore for translocation of secreted proteins. GspD and the inner membrane protein GspC interact with each other via periplasmic domains. Three different crystal structures of the homology region domain of GspC (GspC(HR)) in complex with either two or three domains of the N-terminal region of GspD from enterotoxigenic Escherichia coli show that GspC(HR) adopts an all-β topology. N-terminal β-strands of GspC and the N0 domain of GspD are major components of the interface between these inner and outer membrane proteins from the T2SS. The biological relevance of the observed GspC-GspD interface is shown by analysis of variant proteins in two-hybrid studies and by the effect of mutations in homologous genes on extracellular secretion and subcellular distribution of GspC in Vibrio cholerae. Substitutions of interface residues of GspD have a dramatic effect on the focal distribution of GspC in V. cholerae. These studies indicate that the GspC(HR)-GspD(N0) interactions observed in the crystal structure are essential for T2SS function. Possible implications of our structures for the stoichiometry of the T2SS and exoprotein secretion are discussed.
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