Structure of the outer membrane complex of a type IV secretion system - Archive ouverte HAL Access content directly
Journal Articles Nature Year : 2009

Structure of the outer membrane complex of a type IV secretion system

(1) , (1) , (2) , (1) , (3) , (1)
1
2
3

Abstract

Type IV secretion systems are secretion nanomachines spanning the two membranes of Gram-negative bacteria. Three proteins, VirB7, VirB9 and VirB10, assemble into a 1.05 megadalton (MDa) core spanning the inner and outer membranes. This core consists of 14 copies of each of the proteins and forms two layers, the I and O layers, inserting in the inner and outer membrane, respectively. Here we present the crystal structure of a $\sim$0.6 MDa outer-membrane complex containing the entire O-layer. This structure is the largest determined for an outer-membrane channel and is unprecedented in being composed of three proteins. Unexpectedly, this structure identifies VirB10 as the outer-membrane channel with a unique hydrophobic double-helical transmembrane region. This structure establishes VirB10 as the only known protein crossing both membranes of Gram-negative bacteria. Comparison of the cryo-electron microscopy (cryo-EM) and crystallographic structures points to conformational changes regulating channel opening and closing
Fichier principal
Vignette du fichier
chand.pdf (1.74 Mo) Télécharger le fichier
Origin : Publisher files allowed on an open archive
Loading...

Dates and versions

cea-00909632 , version 1 (15-10-2019)

Identifiers

Cite

Vidya Chandran, Rémi Fronzes, Stéphane Duquerroy, Nora Cronin, Jorge Navaza, et al.. Structure of the outer membrane complex of a type IV secretion system. Nature, 2009, 462 (7276), pp.1011-1015. ⟨10.1038/nature08588⟩. ⟨cea-00909632⟩
95 View
40 Download

Altmetric

Share

Gmail Facebook Twitter LinkedIn More