ArticleNature structural & molecular biology2018
Structure of the core of the type III secretion system export apparatus.
Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 102 papers.
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Who cites it
102 citing papers in PubMed, 178 citations in OpenAlex.
- Protein Structure Characters in the Light of Phylogenetic Systematics.Genome biology and evolution · 2026Article
- Contributions of conserved and species-specific CagX (VirB9) domains to the assembly and function of theInfection and immunity · 2026Article
- Structure of the proton-powered secretion motor at the heart of the bacterial flagellum.bioRxiv : the preprint server for biology · 2026Article
- The last bacterial common ancestor encoded a complex flagellum.bioRxiv : the preprint server for biology · 2026Article
- Engineering Pseudomonas protegens as a Targeted Antifungal-Effector Delivery Chassis via Heterologous Type III Secretion System Reconstitution.Microbial biotechnology · 2026Article
- Article
- Bradyrhizobium dasycarpae sp. nov. a novel rhizobial species lacking canonical nod genes, isolated from the Moroccan endemic legume Retama dasycarpa.Antonie van Leeuwenhoek · 2026Article
- Calcium controls type III secretion switch through an SctV-SctW interplay.Frontiers in microbiology · 2026Article
- Uncoupling substrate delivery from export gate activation reveals distinct roles of the flagellar ATPase complex.Frontiers in microbiology · 2026Article
- Continuous exchange of an inner-membrane ring component is required for assembly and function of the type III secretion system.Nature communications · 2025Article
- Article
- Genome-Based In Silico Analysis of the Structural and Functional Characteristics of the Type Three Secretion System (T3SS) and Core Effector Proteins in EnteropathogenicPathogens (Basel, Switzerland) · 2025Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- A β-cap on the FliPQR protein-export channel acts as the cap for initial flagellar rod assembly.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- FliO is an evolutionarily conserved yet diversified core component of the bacterial flagellar type III secretion system.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The predicted sorting platform dynamically associates with the type III secretion system from Xanthomonas euvesicatoria in response to the external pH.BMC microbiology · 2025Article
- Yersinia actively downregulates type III secretion and adhesion at higher cell densities.PLoS pathogens · 2025Article
- Structure and Dynamics of the Bacterial Flagellar Motor Complex.Biomolecules · 2024Review
- FlaG competes with FliS-flagellin complexes for access to FlhA in the flagellar T3SS to controlProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Establishment of Nested PCR for the Detection ofAnimals : an open access journal from MDPI · 2024Article
42 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
Abstract
Export of proteins through type III secretion systems is critical for motility and virulence of many major bacterial pathogens. Three putative integral membrane proteins (FliP, FliQ, FliR) are suggested to form the core of an export gate in the inner membrane, but their structure, assembly and location within the final nanomachine remain unclear. Here, we present the cryoelectron microscopy structure of the Salmonella Typhimurium FliP-FliQ-FliR complex at 4.2 Å. None of the subunits adopt canonical integral membrane protein topologies, and common helix-turn-helix structural elements allow them to form a helical assembly with 5:4:1 stoichiometry. Fitting of the structure into reconstructions of intact secretion systems, combined with cross-linking, localize the export gate as a core component of the periplasmic portion of the machinery. This study thereby identifies the export gate as a key element of the secretion channel and implies that it primes the helical architecture of the components assembling downstream.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.