ArticleMolecular microbiology2014
Conformational dynamics of protein transporter FhaC: large-scale motions of plug helix.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- DeepPath: overcoming data scarcity for protein transition pathway prediction using physics-based deep learning.Chemical science · 2026Article
- First inhibitor of a bacterial two-partner secretion system.bioRxiv : the preprint server for biology · 2026Article
- Article
- Demonstration and Suggestion on the Communication Efficiency of New Media of Environmental Education Based on Ideological and Political Education.International journal of environmental research and public health · 2023Article
- Structural and biophysical characterization of the secreted, β-helical adhesin EtpA of Enterotoxigenic Escherichia coli.PloS one · 2023Article
- Large-Scale Conformational Changes of FhaC Provide Insights Into the Two-Partner Secretion Mechanism.Frontiers in molecular biosciences · 2022Article
- Protein import and export across the bacterial outer membrane.Current opinion in structural biology · 2021Review
- Structural insight into toxin secretion by contact-dependent growth inhibition transporters.eLife · 2020Article
- Structural basis for substrate selection by the translocation and assembly module of the β-barrel assembly machinery.Molecular microbiology · 2017Article
- Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions.Frontiers in cellular and infection microbiology · 2017Review
- Sequential unfolding of the hemolysin two-partner secretion domain from Proteus mirabilis.Protein science : a publication of the Protein Society · 2015Article
- Conserved Omp85 lid-lock structure and substrate recognition in FhaC.Nature communications · 2015Article
- Structure-function analysis reveals that the Pseudomonas aeruginosa Tps4 two-partner secretion system is involved in CupB5 translocation.Protein science : a publication of the Protein Society · 2015Article
- The β-barrel membrane protein insertase machinery from Gram-negative bacteria.Current opinion in structural biology · 2015Review
- Lateral opening and exit pore formation are required for BamA function.Structure (London, England : 1993) · 2014Article
- FhaC takes a bow to FHA in the two-partner do-si-do.Molecular microbiology · 2014Article
- Electrostatic networks control plug stabilization in the PapC usher.Molecular membrane biologyArticle
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8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
FhaC is an integral outer membrane protein of the whooping cough agent Bordetella pertussis that mediates the transport to the cell surface of a major virulence factor, the filamentous haemagglutinin adhesin FHA. The FHA/FhaC pair is a prototypic TpsA/TpsB system of the widespread 'Two-Partner Secretion' pathway, dedicated to the transport of long extracellular proteins in various pathogenic and environmental Gram-negative bacteria. FhaC belongs to the ubiquitous Omp85 superfamily of protein transporters. The X-ray structure of FhaC shows that the transmembrane β-barrel channel hypothesized to serve as the FHA-conducting pore is obstructed by two structural elements conserved among TpsB transporters, an N-terminal α helix and an extracellular loop. Here, we provide evidence for conformational dynamics of FhaC related to the secretion mechanism. Using paramagnetic electron resonance, electrophysiology and in vivo approaches, we showed that FhaC exchanges between open and closed conformations. The interaction with its secretory partner FHA alters this distribution of conformations. The open conformation of FhaC implies a large displacement from the channel of the N-terminal 'plug' helix, which remains in the periplasm during FHA secretion. The membrane environment favours the dynamics of the TpsB transporter.
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