ArticleProceedings of the National Academy of Sciences of the United States of America2024
Structural basis for adhesin secretion by the outer-membrane usher in type 1 pili.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- A cold-responsiveApplied and environmental microbiology · 2026Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- Structures of the Escherichia coli type 1 pilus during pilus rod assembly and after assembly termination.Nature communications · 2025Article
- Structural basis for adhesin secretion by the outer-membrane usher in type 1 pili.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Conformational ensembles inProceedings of the National Academy of Sciences of the United States of America · 2024Article
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Authors and funding
7 authors.
Funding
Abstract
Gram-negative bacteria produce chaperone-usher pathway pili, which are extracellular protein fibers tipped with an adhesive protein that binds to a receptor with stereochemical specificity to determine host and tissue tropism. The outer-membrane usher protein, together with a periplasmic chaperone, assembles thousands of pilin subunits into a highly ordered pilus fiber. The tip adhesin in complex with its cognate chaperone activates the usher to allow extrusion across the outer membrane. The structural requirements to translocate the adhesin through the usher pore from the periplasm to the extracellular space remains incompletely understood. Here, we present a cryoelectron microscopy structure of a quaternary tip complex in the type 1 pilus system from
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