Structure and function of bacterial outer membrane proteins: barrels in a nutshell - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Molecular Microbiology Année : 2000

Structure and function of bacterial outer membrane proteins: barrels in a nutshell

Résumé

The outer membrane protects Gram-negative bacteria against a harsh environment. At the same time, the embedded proteins fulfil a number of tasks that are crucial to the bacterial cell, such as solute and protein translocation, as well as signal transduction. Unlike membrane proteins from all other sources, integral outer membrane proteins do not consist of transmembrane alpha-helices, but instead fold into antiparallel beta-barrels. Over recent years, the atomic structures of several outer membrane proteins, belonging to six families, have been determined. They include the OmpA membrane domain, the OmpX protein, phospholipase A, general porins (OmpF, PhoE), substrate-specific porins (LamB, ScrY) and the TonB-dependent iron siderophore transporters FhuA and FepA. These crystallographic studies have yielded invaluable insight into and decisively advanced the understanding of the functions of these intriguing proteins. Our review is aimed at discussing their common principles and peculiarities as well as open questions associated with them.

Dates et versions

hal-03621348 , version 1 (28-03-2022)

Identifiants

Citer

Ralf Koebnik, Kaspar Locher, Patrick van Gelder. Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Molecular Microbiology, 2000, 37 (2), pp.239-253. ⟨10.1046/j.1365-2958.2000.01983.x⟩. ⟨hal-03621348⟩
7 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More