Structural basis for antibiotic resistance mediated by the Bacillus subtilis ABCF ATPase VmlR.

ABSTRACT: Many Gram-positive pathogenic bacteria employ ribosomal protection proteins (RPPs) to confer resistance to clinically important antibiotics. In Bacillus subtilis, the RPP VmlR confers resistance to lincomycin (Lnc) and the streptogramin A (S_A) antibiotic virginiamycin M (VgM). VmlR is an ATP-binding cassette (ABC) protein of the F type, which, like other antibiotic resistance (ARE) ABCF proteins, is thought to bind to antibiotic-stalled ribosomes and promote dissociation of the drug from its binding site. To investigate the molecular mechanism by which VmlR confers antibiotic resistance, we have determined a cryo-electron microscopy (cryo-EM) structure of an ATPase-deficient B. subtilis VmlR-EQ₂ mutant in complex with a B. subtilis ErmDL-stalled r

SUBMITTER: Crowe-McAuliffe C 

PROVIDER: S-EPMC6130385 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature