Download MendeleyFiber formation across the bacterial outer membrane by the chaperone/usher pathway.
Remaut, H., Tang, C., Henderson, N.S., Pinkner, J.S., Wang, T., Hultgren, S.J., Thanassi, D.G., Waksman, G., Li, H.(2008) Cell 133: 640-652
- PubMed: 18485872
- DOI: https://doi.org/10.1016/j.cell.2008.03.033
- Primary Citation of Related Structures:
2VQI - PubMed Abstract:
Gram-negative pathogens commonly exhibit adhesive pili on their surfaces that mediate specific attachment to the host. A major class of pili is assembled via the chaperone/usher pathway. Here, the structural basis for pilus fiber assembly and secretion performed by the outer membrane assembly platform--the usher--is revealed by the crystal structure of the translocation domain of the P pilus usher PapC and single particle cryo-electron microscopy imaging of the FimD usher bound to a translocating type 1 pilus assembly intermediate. These structures provide molecular snapshots of a twinned-pore translocation machinery in action. Unexpectedly, only one pore is used for secretion, while both usher protomers are used for chaperone-subunit complex recruitment. The translocating pore itself comprises 24 beta strands and is occluded by a folded plug domain, likely gated by a conformationally constrained beta-hairpin. These structures capture the secretion of a virulence factor across the outer membrane of gram-negative bacteria.
Organizational Affiliation:
Institute of Structural Molecular Biology, University College London and Birkbeck College, Malet Street, London, WC1E 7HX, United Kingdom.
