Structure and dynamics of a mycobacterial type VII secretion system.

ABSTRACT: Mycobacterium tuberculosis is the cause of one of the most important infectious diseases in humans, which leads to 1.4 million deaths every year¹. Specialized protein transport systems-known as type VII secretion systems (T7SSs)-are central to the virulence of this pathogen, and are also crucial for nutrient and metabolite transport across the mycobacterial cell envelope^2,3. Here we present the structure of an intact T7SS inner-membrane complex of M. tuberculosis. We show how the 2.32-MDa ESX-5 assembly, which contains 165 transmembrane helices, is restructured and stabilized as a trimer of dimers by the MycP₅ protease. A trimer of MycP₅ caps a central periplasmic dome-like chamber that is formed by three EccB₅ dimers, with the proteol

SUBMITTER: Bunduc CM 

PROVIDER: S-EPMC8131196 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature