ArticleJournal of structural biology2009
The dimer formed by the periplasmic domain of EpsL from the Type 2 Secretion System of Vibrio parahaemolyticus.
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 28 papers.
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Who cites it
28 citing papers in PubMed, 52 citations in OpenAlex.
- Genomic Insight intoPathogens (Basel, Switzerland) · 2025Article
- Transcriptomic analyses of Vibrio parahaemolyticus under the phenyllactic acid stress.Applied microbiology and biotechnology · 2024Article
- Comparative genome analyses of fiveMicrobial genomics · 2022Article
- Crystal structure of monomeric Amuc_1100 from Akkermansia muciniphila.Acta crystallographica. Section F, Structural biology communications · 2020Article
- In vivo structure of the Legionella type II secretion system by electron cryotomography.Nature microbiology · 2019Article
- Assessing the impact, genomics and evolution of type II secretion across a large, medically important genus: the Legionella type II secretion paradigm.Microbial genomics · 2019Article
- Architecture, Function, and Substrates of the Type II Secretion System.EcoSal Plus · 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
- Structure and oligomerization of the periplasmic domain of GspL from the type II secretion system of Pseudomonas aeruginosa.Scientific reports · 2018Article
- Conserved, unstructured regions in Pseudomonas aeruginosa PilO are important for type IVa pilus function.Scientific reports · 2018Article
- Potential Survival and Pathogenesis of a Novel Strain,Frontiers in microbiology · 2018Article
- Article
- Type IV Pilus Alignment Subcomplex Proteins PilN and PilO Form Homo- and Heterodimers in Vivo.The Journal of biological chemistry · 2016Article
- Secretion systems in Gram-negative bacteria: structural and mechanistic insights.Nature reviews. Microbiology · 2015Review
- Exceptionally widespread nanomachines composed of type IV pilins: the prokaryotic Swiss Army knives.FEMS microbiology reviews · 2015Review
- Editorial.FEMS microbiology reviews · 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
- Structure and assembly of an inner membrane platform for initiation of type IV pilus biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- A dodecameric ring-like structure of the N0 domain of the type II secretin from enterotoxigenic Escherichia coli.Journal of structural biology · 2013Article
- PilMNOPQ from the Pseudomonas aeruginosa type IV pilus system form a transenvelope protein interaction network that interacts with PilA.Journal of bacteriology · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The Type 2 Secretion System (T2SS), occurring in many Gram-negative bacteria, is responsible for the transport of a diversity of proteins from the periplasm across the outer membrane into the extracellular space. In Vibrio cholerae, the T2SS secretes several unrelated proteins including the major virulence factor cholera toxin. The T2SS consists of three sub-assemblies, one of which is the Inner Membrane Complex which contains multiple copies of five proteins, including the bitopic membrane protein EpsL. Here, we report the 2.3A resolution crystal structure of the periplasmic domain of EpsL (peri-EpsL) from Vibrio parahaemolyticus, which is 56% identical in sequence to its homolog in V. cholerae. The domain adopts a circular permutation of the "common" ferredoxin fold with two contiguous sub-domains. Remarkably, this infrequently occurring permutation was for the first time observed in the periplasmic domain of EpsM (peri-EpsM), another T2SS protein which interacts with EpsL. These two domains are 18% identical in sequence which may indicate a common evolutionary origin. Both peri-EpsL and peri-EpsM form dimers, but the organization of the subunits in these dimers appears to be entirely different. We have previously shown that the cytoplasmic domain of EpsL is also dimeric and forms a heterotetramer with the first domain of the "secretion ATPase" EpsE. The latter enzyme is most likely hexameric. The possible consequences of the combination of the different symmetries of EpsE and EpsL for the architecture of the T2SS are discussed.
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