期刊
CELL
卷 133, 期 4, 页码 640-652出版社
CELL PRESS
DOI: 10.1016/j.cell.2008.03.033
关键词
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资金
- Medical Research Council [G0800002, 58149] Funding Source: Medline
- NIAID NIH HHS [R01 AI048689-08, AI48689, R37 AI029549, R37 AI048689, R01 AI029549, R01 AI049950, AI029549, R01 AI048689, AI049950] Funding Source: Medline
- NIGMS NIH HHS [R01 GM062987, R01 GM074985, GM074985, GM062987] Funding Source: Medline
- Medical Research Council [G0800002] Funding Source: researchfish
- MRC [G0800002] Funding Source: UKRI
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.
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