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-Structure paper
Title | Fiber formation across the bacterial outer membrane by the chaperone/usher pathway. |
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Journal, issue, pages | Cell, Vol. 133, Issue 4, Page 640-652, Year 2008 |
Publish date | May 16, 2008 |
Authors | Han Remaut / Chunyan Tang / Nadine S Henderson / Jerome S Pinkner / Tao Wang / Scott J Hultgren / David G Thanassi / Gabriel Waksman / Huilin Li / |
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 ...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. |
External links | Cell / PubMed:18485872 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 3.2 - 23.0 Å |
Structure data | EMDB-5009: PDB-2vqi: |
Chemicals | ChemComp-LDA: ChemComp-C8E: ChemComp-HOH: |
Source |
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Keywords | TRANSPORT / TRANSMEMBRANE / OUTER MEMBRANE / USHER / P PILUS / MEMBRANE / FIMBRIUM / OM TRANSLOCATION PORE / PILUS ASSEMBLY PLATFORM |