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- W4285012019 abstract "Abstract Efflux of antibacterial compounds is a major mechanism for developing antimicrobial resistance. In the Gram-positive pathogen Staphylococcus aureus , QacA, a 14 transmembrane (TM) helix containing major facilitator superfamily antiporter, mediates proton-coupled efflux of mono and divalent cationic antibacterial compounds. In this study, we report the cryoEM structure of QacA, with a single mutation D411N that improves homogeneity and retains efflux activity against divalent cationic compounds like dequalinium and chlorhexidine. The structure of substrate-free QacA, complexed to two single-domain camelid antibodies, was elucidated to a resolution of 3.6 Å. The structure displays an outward-open conformation with an extracellular hairpin loop, which is conserved in a subset of DHA2 transporters and its deletion causes a loss of function in the transporter. Modeling and simulations of QacA’s cytosol-facing and occluded conformations reveal asymmetry in the rocker-switch mode of QacA’s conformational shifts, providing new insights into the organization and structural dynamics of DHA2 members." @default.
- W4285012019 created "2022-07-12" @default.
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- W4285012019 date "2022-07-10" @default.
- W4285012019 modified "2023-10-14" @default.
- W4285012019 title "CryoEM structure of QacA, an antibacterial efflux transporter from <i>Staphylococcus aureus</i>" @default.
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- W4285012019 doi "https://doi.org/10.1101/2022.07.09.499445" @default.
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