8qoe
From Proteopedia
Jump to navigationJump to search
Inward-facing conformation of the ABC transporter BmrA
| ||||||||||||
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
| ||||||||||||||||||
This page was last modified 10:04, 20 December 2023.