9h8n
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Structure of BmrA T123C-S428C reduced form (apo state)
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Structural highlights
FunctionBMRA_BACSU An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation (PubMed:18215075). Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable).[1] References
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This page was last modified 03:38, 14 May 2026.