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ProteomicsStructural insights into the catalytic cycle of a bacterial multidrug ABC efflux pump
ABC (“ATP-Binding Cassette”) exporters of the type IV subfamily gather transporters involved in the efflux of many compounds and notably those capable to confer multidrug resistance like the mammalian P-glycoprotein or the bacterial transporter BmrA. They function according to an alternating access ...
ORGANISM(S): Bacillus subtilis 
2022-03-24 | PXD028663 | Pride
Multidrug resistance Hydrogen-deuterium exchange ms Abc transporter Bmra 
ProteomicsHDX-MS studies of the bacterial multidrug ABC transporter BmrA in presence or absence of a ligand (rhodamine-6G)
Multidrug ATP-Binding Cassette (ABC) exporters use an alternating access mechanism to translocate drugs across membranes, but the molecular mechanism of substrate release is still elusive due to the poor affinity of the drug-binding pocket for its ligand at this stage. Here, we bring new information...
ORGANISM(S): Bacillus subtilis 
2022-01-27 | PXD027447 | Pride
Bmra Abc transporter Hydrogen-deuterium ms 
UnknownThe C-terminal α-helix is crucial for the activity of the bacterial ABC transporter BmrA.
Not available
S-EPMC11774805 | biostudies-literature
UnknownStubborn contaminants: influence of detergents on the purity of the multidrug ABC transporter BmrA.
Not available
S-EPMC4269414 | biostudies-literature
UnknownSolid-State NMR Reveals Asymmetric ATP Hydrolysis in the Multidrug ABC Transporter BmrA.
Not available
S-EPMC9284561 | biostudies-literature
UnknownRhodamine6G and Hœchst33342 narrow BmrA conformational spectrum for a more efficient use of ATP.
Not available
S-EPMC11836358 | biostudies-literature
UnknownUnfolding Individual Domains of BmrA, a Bacterial ABC Transporter Involved in Multidrug Resistance.
Not available
S-EPMC10049088 | biostudies-literature
UnknownEfficient and stable reconstitution of the ABC transporter BmrA for solid-state NMR studies.
Not available
S-EPMC4428385 | biostudies-literature
UnknownProbing the conformation of the resting state of a bacterial multidrug ABC transporter, BmrA, by a site-directed spin labeling approach.
Not available
S-EPMC2775218 | biostudies-literature
UnknownBackbone NMR assignment of the nucleotide binding domain of the Bacillus subtilis ABC multidrug transporter BmrA in the post-hydrolysis state.
Not available
S-EPMC9068644 | biostudies-literature
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