ArticleJournal of molecular biology2008
Structure of the minor pseudopilin EpsH from the Type 2 secretion system of Vibrio cholerae.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 50 citations in OpenAlex.
- Expression of soluble Type IV Minor Pilins and isolation of abioRxiv : the preprint server for biology · 2026Article
- The molecular basis of FimT-mediated DNA uptake during bacterial natural transformation.Nature communications · 2022Article
- Population genomics of the food-borne pathogenMicrobial genomics · 2022Article
- Virulence Regulation and Innate Host Response in the Pathogenicity ofFrontiers in cellular and infection microbiology · 2020Review
- Architecture, Function, and Substrates of the Type II Secretion System.EcoSal Plus · 2019Review
- Structure-guided disruption of the pseudopilus tip complex inhibits the Type II secretion in Pseudomonas aeruginosa.PLoS pathogens · 2018Article
- Complete genome sequence of Vibrio vulnificus FORC_017 isolated from a patient with a hemorrhagic rash after consuming raw dotted gizzard shad.Gut pathogens · 2016Article
- High-resolution structure of a type IV pilin from the metal-reducing bacterium Shewanella oneidensis.BMC structural biology · 2015Article
- Pseudomonas aeruginosa minor pilins prime type IVa pilus assembly and promote surface display of the PilY1 adhesin.The Journal of biological chemistry · 2015Article
- Crystal structure of the full-length ATPase GspE from the Vibrio vulnificus type II secretion system in complex with the cytoplasmic domain of GspL.Journal of structural biology · 2014Article
- Type IV pilin proteins: versatile molecular modules.Microbiology and molecular biology reviews : MMBR · 2012Review
- On the path to uncover the bacterial type II secretion system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- The type II secretion system: biogenesis, molecular architecture and mechanism.Nature reviews. Microbiology · 2012Review
- Structural insights into the Type II secretion nanomachine.Current opinion in structural biology · 2012Review
- Type II secretion in Yersinia-a secretion system for pathogenicity and environmental fitness.Frontiers in cellular and infection microbiology · 2012Review
- The assembly mode of the pseudopilus: a hallmark to distinguish a novel secretion system subtype.The Journal of biological chemistry · 2011Article
- In vivo cross-linking of EpsG to EpsL suggests a role for EpsL as an ATPase-pseudopilin coupling protein in the Type II secretion system of Vibrio cholerae.Molecular microbiology · 2011Article
- Structure of the minor pseudopilin XcpW from the Pseudomonas aeruginosa type II secretion system.Acta crystallographica. Section D, Biological crystallography · 2011Article
- Structure of the cholera toxin secretion channel in its closed state.Nature structural & molecular biology · 2010Article
- Toxins from bacteria.EXS · 2010Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Many Gram-negative bacteria use the multi-protein type II secretion system (T2SS) to selectively translocate virulence factors from the periplasmic space into the extracellular environment. In Vibrio cholerae the T2SS is called the extracellular protein secretion (Eps) system,which translocates cholera toxin and several enzymes in their folded state across the outer membrane. Five proteins of the T2SS, the pseudopilins, are thought to assemble into a pseudopilus, which may control the outer membrane pore EpsD, and participate in the active export of proteins in a "piston-like" manner. We report here the 2.0 A resolution crystal structure of an N-terminally truncated variant of EpsH, a minor pseudopilin from Vibrio cholerae. While EpsH maintains an N-terminal alpha-helix and C-terminal beta-sheet consistent with the type 4a pilin fold, structural comparisons reveal major differences between the minor pseudopilin EpsH and the major pseudopilin GspG from Klebsiella oxytoca: EpsH contains a large beta-sheet in the variable domain, where GspG contains an alpha-helix. Most importantly, EpsH contains at its surface a hydrophobic crevice between its variable and conserved beta-sheets, wherein a majority of the conserved residues within the EpsH family are clustered. In a tentative model of a T2SS pseudopilus with EpsH at its tip, the conserved crevice faces away from the helix axis. This conserved surface region may be critical for interacting with other proteins from the T2SS machinery.
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