ArticleJournal of structural biology2009
The three-dimensional structure of the cytoplasmic domains of EpsF from the type 2 secretion system of Vibrio cholerae.
Article in Journal of structural biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Integrative Structure and Function of thebioRxiv : the preprint server for biology · 2025Article
- Modularization of the type II secretion gene cluster from Xanthomonas euvesicatoria facilitates the identification of a structurally conserved XpsCLM assembly platform complex.PLoS pathogens · 2025Article
- How Does the Archaellum Work?Biomolecules · 2025Review
- Article
- Membrane platform protein PulF of themBio · 2024Article
- Review
- Mechanism of assembly of type 4 filaments: everything you always wanted to know (but were afraid to ask).Microbiology (Reading, England) · 2023Review
- Article
- Landmark Discoveries and Recent Advances in Type IV Pilus Research.Microbiology and molecular biology reviews : MMBR · 2022Review
- 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
- Architecture, Function, and Substrates of the Type II Secretion System.EcoSal Plus · 2019Review
- Relationship Between Quorum Sensing and Secretion Systems.Frontiers in microbiology · 2019Review
- A Hybrid Secretion System Facilitates Bacterial Sporulation: A Structural Perspective.Microbiology spectrum · 2019Review
- Direct interactions between the secreted effector and the T2SS components GspL and GspM reveal a new effector-sensing step during type 2 secretion.The Journal of biological chemistry · 2018Article
- Structural characterization of SpoIIIAB sporulation-essential protein in Bacillus subtilis.Journal of structural biology · 2018Article
- Unraveling the Self-Assembly of themBio · 2017Article
- Near-atomic resolution cryoelectron microscopy structure of the 30-fold homooligomeric SpoIIIAG channel essential to spore formation inProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Molecular Insights into Pathogenesis and Infection withThe Malaysian journal of medical sciences : MJMS · 2017Review
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7 authors.
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Abstract
The type 2 secretion system (T2SS), a multi-protein machinery that spans both the inner and the outer membranes of Gram-negative bacteria, is used for the secretion of several critically important proteins across the outer membrane. Here we report the crystal structure of the N-terminal cytoplasmic domain of EpsF, an inner membrane spanning T2SS protein from Vibrio cholerae. This domain consists of a bundle of six anti-parallel helices and adopts a fold that has not been described before. The long C-terminal helix alpha6 protrudes from the body of the domain and most likely continues as the first transmembrane helix of EpsF. Two N-terminal EpsF domains form a tight dimer with a conserved interface, suggesting that the observed dimer occurs in the T2SS of many bacteria. Two calcium binding sites are present in the dimer interface with ligands provided for each site by both subunits. Based on this new structure, sequence comparisons of EpsF homologs and localization studies of GFP fused with EpsF, we propose that the second cytoplasmic domain of EpsF adopts a similar fold as the first cytoplasmic domain and that full-length EpsF, and its T2SS homologs, have a three-transmembrane helix topology.
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