The transport activity of the multidrug ABC transporter BmrA does not require a wide separation of the nucleotide-binding domains.

ABSTRACT: ATP-binding cassette (ABC) transporters are ubiquitous membrane proteins responsible for the translocation of a wide diversity of substrates across biological membranes. Some of them confer multidrug or antimicrobial resistance to cancer cells and pathogenic microorganisms, respectively. Despite a wealth of structural data gained in the last two decades, the molecular mechanism of these multidrug efflux pumps remains elusive, including the extent of separation between the two nucleotide-binding domains (NBDs) during the transport cycle. Based on recent outward-facing structures of BmrA, a homodimeric multidrug ABC transporter from Bacillus subtilis, we introduced a cysteine mutation near the C-terminal end of the NBDs to analyze the impact of disulfide-bond formation on BmrA function. Inte

SUBMITTER: Di Cesare M 

PROVIDER: S-EPMC10821409 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature