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TitleStructural insights into the secretin complex of a type IVb pilus system.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 9136, Year 2025
Publish dateOct 16, 2025
AuthorsChenchen Pei / Hui Sun / Yinliang Qi / Xiaomei Li / Zhixiong Fang / Manjuan Tang / Rujing Zhang / Zhaofeng Yan / Meng Yin /
PubMed AbstractThe bundle-forming pilus (BFP) system in enteropathogenic Escherichia coli (EPEC) produces type IVb pili that enable bacterial auto-aggregation, facilitating bacterial adhesion, colonization, and ...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.
External linksNat Commun / PubMed:41102207 / PubMed Central
MethodsEM (single particle)
Resolution2.56 Å
Structure data

63882

9u5s

EMDB-63882, PDB-9u5s:
The structure of the BfpBG complex in the T4bP system
Method: EM (single particle) / Resolution: 2.56 Å

Source
  • Escherichia coli O127:H6 (strain E2348/69 / EPEC) (bacteria)
  • escherichia coli o127:h6 str. e2348/69 (bacteria)
KeywordsPROTEIN TRANSPORT / SECRETIN FAMILY / C17 SYMMETRY / T4bP

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