ArticleNature communications2020
The substrate specificity switch FlhB assembles onto the export gate to regulate type three secretion.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed.
- Protein Structure Characters in the Light of Phylogenetic Systematics.Genome biology and evolution · 2026Article
- Active removal of inhibitory components drives the flagellar type 3 secretion-specificity switch.mBio · 2026Article
- Structure of the proton-powered secretion motor at the heart of the bacterial flagellum.bioRxiv : the preprint server for biology · 2026Article
- Active removal of inhibitory components drives the flagellar Type III Secretion Specificity Switch.bioRxiv : the preprint server for biology · 2026Article
- Uncoupling substrate delivery from export gate activation reveals distinct roles of the flagellar ATPase complex.Frontiers in microbiology · 2026Article
- Calcium controls type III secretion switch through an SctV-SctW interplay.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
- 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
- The predicted sorting platform dynamically associates with the type III secretion system from Xanthomonas euvesicatoria in response to the external pH.BMC microbiology · 2025Article
- Probabilistic single-particle cryo-EM ab initio 3D reconstruction in SIMPLE.Acta crystallographica. Section D, Structural biology · 2025Article
- Transcriptomic insights into slyA-mediated regulation of motility and secretion in Escherichia coli.Antonie van Leeuwenhoek · 2025Article
- Structure and Dynamics of the Bacterial Flagellar Motor Complex.Biomolecules · 2024Review
- The two-component system CpxA/CpxR regulates pathogenesis and stress adaptability in the poplar canker bacterium Lonsdalea populi.Molecular plant pathology · 2024Article
- 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
- Loss to gain: pseudogenes in microorganisms, focusing on eubacteria, and their biological significance.Applied microbiology and biotechnology · 2024Review
- Helicobacter pylori FlgN binds its substrate FlgK and the flagellum ATPase FliI in a similar manner observed for the FliT chaperone.Protein science : a publication of the Protein Society · 2024Article
- Blue Native PAGE Analysis of Bacterial Secretion Complexes.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Structure, Assembly, and Function of Flagella Responsible for Bacterial Locomotion.EcoSal Plus · 2023Review
- Parallel genetic adaptation ofMicrobial genomics · 2023Article
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10 authors.
Funding
Abstract
Protein secretion through type-three secretion systems (T3SS) is critical for motility and virulence of many bacteria. Proteins are transported through an export gate containing three proteins (FliPQR in flagella, SctRST in virulence systems). A fourth essential T3SS protein (FlhB/SctU) functions to "switch" secretion substrate specificity once the growing hook/needle reach their determined length. Here, we present the cryo-electron microscopy structure of an export gate containing the switch protein from a Vibrio flagellar system at 3.2 Å resolution. The structure reveals that FlhB/SctU extends the helical export gate with its four predicted transmembrane helices wrapped around FliPQR/SctRST. The unusual topology of the FlhB/SctU helices creates a loop wrapped around the bottom of the closed export gate. Structure-informed mutagenesis suggests that this loop is critical in gating secretion and we propose that a series of conformational changes in the T3SS trigger opening of the gate through interactions between FlhB/SctU and FliPQR/SctRST.
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