ArticleJournal of structural biology2014
Crystal structure of the full-length ATPase GspE from the Vibrio vulnificus type II secretion system in complex with the cytoplasmic domain of GspL.
Article in Journal of structural biology, 2014. 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, 37 citations in OpenAlex.
- A broad-spectrum phage-encoded mechanism to disarm bacterial type IV filaments.PLoS pathogens · 2026Article
- A broad-spectrum phage-encoded mechanism to disarm bacterial type IV filaments.bioRxiv : the preprint server for biology · 2026Article
- 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
- Building permits-control of type IV pilus assembly by PilB and its cofactors.Journal of bacteriology · 2024Review
- Mechanism of assembly of type 4 filaments: everything you always wanted to know (but were afraid to ask).Microbiology (Reading, England) · 2023Review
- Article
- The PilB-PilZ-FimX regulatory complex of the Type IV pilus from Xanthomonas citri.PLoS pathogens · 2021Article
- Analysis of diverse eukaryotes suggests the existence of an ancestral mitochondrial apparatus derived from the bacterial type II secretion system.Nature communications · 2021Article
- Secrete or perish: The role of secretion systems inComputational and structural biotechnology journal · 2021Review
- Core architecture of a bacterial type II secretion system.Nature communications · 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
- The Dynamic Structures of the Type IV Pilus.Microbiology spectrum · 2019Review
- 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
- Structural cycle of the Thermus thermophilus PilF ATPase: the powering of type IVa pilus assembly.Scientific reports · 2018Article
- Unraveling the Self-Assembly of themBio · 2017Article
- Reconstitution of a minimal machinery capable of assembling periplasmic type IV pili.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Cyclic Di-GMP Binding by an Assembly ATPase (PilB2) and Control of Type IV Pilin Polymerization in the Gram-Positive Pathogen Clostridium perfringens.Journal of bacteriology · 2017Article
- Identification of New Virulence Factors and Vaccine Candidates forFrontiers in cellular and infection microbiology · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
The type II secretion system (T2SS) is present in many Gram-negative bacteria and is responsible for secreting a large number of folded proteins, including major virulence factors, across the outer membrane. The T2SS consists of 11-15 different proteins most of which are present in multiple copies in the assembled secretion machinery. The ATPase GspE, essential for the functioning of the T2SS, contains three domains (N1E, N2E and CTE) of which the N1E domain is associated with the cytoplasmic domain of the inner membrane protein GspL. Here we describe and analyze the structure of the GspE•cyto-GspL complex from Vibrio vulnificus in the presence of an ATP analog, AMPPNP. There are three such ∼83 kDa complexes per asymmetric unit with essentially the same structure. The N2E and CTE domains of a single V. vulnificus GspE subunit adopt a mutual orientation that has not been seen before in any of the previous GspE structures, neither in structures of related ATPases from other secretion systems. This underlines the tremendous conformational flexibility of the T2SS secretion ATPase. Cyto-GspL interacts not only with the N1E domain, but also with the CTE domain and is even in contact with AMPPNP. Moreover, the cyto-GspL domains engage in two types of mutual interactions, resulting in two essentially identical, but crystallographically independent, "cyto-GspL rods" that run throughout the crystal. Very similar rods are present in previous crystals of cyto-GspL and of the N1E•cyto-GspL complex. This arrangement, now seen four times in three entirely different crystal forms, involves contacts between highly conserved residues suggesting a role in the biogenesis or the secretion mechanism or both of the T2SS.
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