ArticleJournal of molecular biology2008
The crystal structure of a binary complex of two pseudopilins: EpsI and EpsJ from the type 2 secretion system of Vibrio vulnificus.
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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29 citing papers in PubMed, 48 citations in OpenAlex.
- β-strand addition within tip initiation complexes licenses assembly of diverse type IV filaments.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- β-strand complementation within tip initiation complexes licenses assembly of diverse type IV filaments.bioRxiv : the preprint server for biology · 2026Article
- Proteomic Analysis of the Fish PathogenAnimals : an open access journal from MDPI · 2024Article
- Characterization of a glycan-binding complex of minor pilins completes the analysis ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Role of Minor Pilins in Assembly and Function of the Competence Pilus ofFrontiers in cellular and infection microbiology · 2021Article
- Structure-guided disruption of the pseudopilus tip complex inhibits the Type II secretion in Pseudomonas aeruginosa.PLoS pathogens · 2018Article
- Structures of type IV pilins from Thermus thermophilus demonstrate similarities with type II secretion system pseudopilins.Journal of structural biology · 2016Article
- Crystal Structure of the Minor Pilin CofB, the Initiator of CFA/III Pilus Assembly in Enterotoxigenic Escherichia coli.The Journal of biological chemistry · 2015Article
- 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
- Complex formation and processing of the minor transformation pilins of Bacillus subtilis.Molecular microbiology · 2013Article
- Split green fluorescent protein as a modular binding partner for protein crystallization.Acta crystallographica. Section D, Biological crystallography · 2013Article
- 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
- Improvement of the crystallizability and expression of an RNA crystallization chaperone.Journal of biochemistry · 2011Article
- Antibody fragments as tools in crystallography.Clinical and experimental immunology · 2011Review
- The assembly mode of the pseudopilus: a hallmark to distinguish a novel secretion system subtype.The Journal of biological chemistry · 2011Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Type II secretion systems (T2SS) translocate virulence factors from the periplasmic space of many pathogenic bacteria into the extracellular environment. The T2SS of Vibrio cholerae and related species is called the extracellular protein secretion (Eps) system that consists of a core of multiple copies of 11 different proteins. The pseudopilins, EpsG, EpsH, EpsI, EpsJ and EpsK, are five T2SS proteins that are thought to assemble into a pseudopilus, which is assumed to interact with the outer membrane pore, and may actively participate in the export of proteins. We report here biochemical evidence that the minor pseudopilins EpsI and EpsJ from Vibrio species interact directly with one another. Moreover, the 2.3 A resolution crystal structure of a complex of EspI and EpsJ from Vibrio vulnificus represents the first atomic resolution structure of a complex of two different pseudopilin components from the T2SS. Both EpsI and EpsJ appear to be structural extremes within the family of type 4a pilin structures solved to date, with EpsI having the smallest, and EpsJ the largest, "variable pilin segment" seen thus far. A high degree of sequence conservation in the EpsI:EpsJ interface indicates that this heterodimer occurs in the T2SS of a large number of bacteria. The arrangement of EpsI and EpsJ in the heterodimer would correspond to a right-handed helical character of proteins assembled into a pseudopilus.
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