PMID:18485872
| Citation |
Remaut, H, Tang, C, Henderson, NS, Pinkner, JS, Wang, T, Hultgren, SJ, Thanassi, DG, Waksman, G and Li, H (2008) Fiber formation across the bacterial outer membrane by the chaperone/usher pathway. Cell 133:640-52 |
|---|---|
| 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. |
| Links |
PubMed PMC3036173 Online version:10.1016/j.cell.2008.03.033 |
| Keywords |
Amino Acid Sequence; Biosynthetic Pathways; Crystallography, X-Ray; Escherichia coli/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Escherichia coli Proteins/ultrastructure; Fimbriae Proteins/chemistry; Fimbriae Proteins/metabolism; Fimbriae Proteins/ultrastructure; Fimbriae, Bacterial/ultrastructure; Models, Molecular; Molecular Chaperones/metabolism; Molecular Sequence Data; Multiprotein Complexes/chemistry; Multiprotein Complexes/metabolism; Porins/chemistry; Porins/metabolism |
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