ArticlePloS one2021
Nonameric structures of the cytoplasmic domain of FlhA and SctV in the context of the full-length protein.
Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 30 citations in OpenAlex.
- Structure of the proton-powered secretion motor at the heart of the bacterial flagellum.bioRxiv : the preprint server for biology · 2026Article
- Calcium controls type III secretion switch through an SctV-SctW interplay.Frontiers in microbiology · 2026Article
- Structural basis for substrate specificity switching revealed by the FlhA(A489E) suppressor mutation.Biophysics and physicobiology · 2026Article
- 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
- 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
- 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
- FliH and FliI help FlhA bring strict order to flagellar protein export in Salmonella.Communications biology · 2024Article
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- Primary architecture and energy requirements of Type III and Type IV secretion systems.Frontiers in cellular and infection microbiology · 2023Review
- The Vibrio Polar Flagellum: Structure and Regulation.Advances in experimental medicine and biology · 2023Article
- Crystals of SctV from different species reveal variable symmetry for the cytosolic domain of the type III secretion system export gate.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Conserved GYXLI Motif of FlhA Is Involved in Dynamic Domain Motions of FlhA Required for Flagellar Protein Export.Microbiology spectrum · 2022Article
- Cryo-EM of the injectisome and type III secretion systems.Current opinion in structural biology · 2022Review
- Direct interaction of a chaperone-bound type III secretion substrate with the export gate.Nature communications · 2022Article
- Type III secretion by Yersinia pseudotuberculosis is reliant upon an authentic N-terminal YscX secretor domain.Molecular microbiology · 2022Article
- Activation mechanism of the bacterial flagellar dual-fuel protein export engine.Biophysics and physicobiology · 2022Article
- Insight Into Distinct Functional Roles of the Flagellar ATPase Complex for Flagellar Assembly inFrontiers in microbiology · 2022Review
- Structural and Functional Analysis of SsaV Cytoplasmic Domain and Variable Linker States in the Context of the InvA-SsaV Chimeric Protein.Microbiology spectrum · 2021Article
- Structure of the cytoplasmic domain of SctV (SsaV) from the Salmonella SPI-2 injectisome and implications for a pH sensing mechanism.Journal of structural biology · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
Type three secretion is the mechanism of protein secretion found in bacterial flagella and injectisomes. At its centre is the export apparatus (EA), a complex of five membrane proteins through which secretion substrates pass the inner membrane. While the complex formed by four of the EA proteins has been well characterised structurally, little is known about the structure of the membrane domain of the largest subunit, FlhA in flagella, SctV in injectisomes. Furthermore, the biologically relevant nonameric assembly of FlhA/SctV has been infrequently observed and differences in conformation of the cytoplasmic portion of FlhA/SctV between open and closed states have been suggested to reflect secretion system specific differences. FlhA has been shown to bind to chaperone-substrate complexes in an open state, but in previous assembled ring structures, SctV is in a closed state. Here, we identify FlhA and SctV homologues that can be recombinantly produced in the oligomeric state and study them using cryo-electron microscopy. The structures of the cytoplasmic domains from both FlhA and SctV are in the open state and we observe a conserved interaction between a short stretch of residues at the N-terminus of the cytoplasmic domain, known as FlhAL/SctVL, with a groove on the adjacent protomer's cytoplasmic domain, which stabilises the nonameric ring assembly.
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