Oligomerization is required for channel formation of MctB and for copper resistance of Mycobacterium tuberculosis.

ABSTRACT: The mammalian immune system kills bacterial pathogens including Mycobacterium tuberculosis by increasing copper uptake into the phagosome of infected macrophages. Rv1698 was previously identified as a membrane-spanning channel protein. The rv1698 deletion mutant of M. tuberculosis accumulated 100-fold more copper and lungs of infected guinea pigs had a 1000-fold reduced bacterial burden compared to the WT strain. Thus, Rv1698 is an important virulence factor and was named mycobacterial copper transport protein B (MctB). However, the mechanism by which MctB confers copper resistance is unknown. Here, we solved the crystal structure of MctB which revealed a ∼7 nm long helix followed by a large globular Rossmann-like domain. Subsequent experiments showed that the N-terminal hydrophobic helix

SUBMITTER: Siroy A 

PROVIDER: S-EPMC12859517 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature