2VQI

Structure of the P pilus usher (PapC) translocation pore

2VQI の概要

• エントリーDOI: 10.2210/pdb2vqi/pdb
• 分子名称: OUTER MEMBRANE USHER PROTEIN PAPC, LAURYL DIMETHYLAMINE-N-OXIDE, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, ... (4 entities in total)
• 機能のキーワード: transmembrane, outer membrane, transport, usher, p pilus, membrane, fimbrium, om translocation pore, pilus assembly platform
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 116329.65

構造登録者

Remaut, H.,Tang, C.,Henderson, N.S.,Pinkner, J.S.,Wang, T.,Hultgren, S.J.,Thanassi, D.G.,Li, H.,Waksman, G. (登録日: 2008-03-16, 公開日: 2008-05-27, 最終更新日: 2019-01-16)

主引用文献

Remaut, H.,Tang, C.,Henderson, N.S.,Pinkner, J.S.,Wang, T.,Hultgren, S.J.,Thanassi, D.G.,Waksman, G.,Li, H.
Fiber formation across the bacterial outer membrane by the chaperone/usher pathway.
Cell, 133:640-652, 2008

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.

PubMed: 18485872
DOI: 10.1016/j.cell.2008.03.033

実験手法

X-RAY DIFFRACTION (3.2 Å)