ArticleNature communications2025
Structural insights into the secretin complex of a type IVb pilus system.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Beyond structure: spectroscopic imaging in cryogenic electron microscopy.Current opinion in structural biology · 2026Review
- Antioxidation is a Common Defense Strategy for Different Species Under Mechanical Stress.Advanced genetics (Hoboken, N.J.) · 2026Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bundle-forming pilus (BFP) system in enteropathogenic Escherichia coli (EPEC) produces type IVb pili that enable bacterial auto-aggregation, facilitating bacterial adhesion, colonization, and virulence. One of its components, lipoprotein BfpB, interacts with BfpG to form a secretin channel complex that enables pilus translocation across the outer membrane. Here, we report a high-resolution cryo-EM structure of the BfpB-BfpG complex, revealing a 17:17 stoichiometry with stable zigzag-like interactions between BfpG and BfpB near the N3 ring. Secretin BfpB consists of three β-barrels, including an additional N3 barrel that is crucial for BFP biogenesis. As a lipoprotein-type secretin, BfpB possesses an N-terminal LG domain that bridges the N0 domain and the outer membrane, ensuring its correct localization to the bacterial outer membrane. The C-terminal region of the LG domain mediates binding to BfpG, and disruption of these interactions impairs BFP biogenesis. Our results advance our understanding of the assembly mechanism of secretin complexes within the secretin superfamily.
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Registered trials
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