Structural highlights
Function
BMRA_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
- ↑ Orelle C, Gubellini F, Durand A, Marco S, Levy D, Gros P, Di Pietro A, Jault JM. Conformational change induced by ATP binding in the multidrug ATP-binding cassette transporter BmrA. Biochemistry. 2008 Feb 26;47(8):2404-12. doi: 10.1021/bi702303s. Epub 2008 Jan, 24. PMID:18215075 doi:http://dx.doi.org/10.1021/bi702303s
