3.A.1.106.2
The homodimeric Sav1866 multidrug exporter (transports doxorubicin, verapamil, ethidium, tetraphenylphosphonium, vinblastine and the fluorescent dye, Hoechst 33342; 3-D structure known at 3 Å resolution; Dawson and Locher, 2006; Velamakanni et al., 2008) The empty site opens by rotation of the nucleotide-binding domain whereas the ATP-bound site remains occluded (Jones and George, 2011). Conformational changes induced by ATP-binding and hydrolysis have been proposed (Becker et al. 2010; Oliveira et al., 2011). The alternating access mechanism and the flippase activity of this ABC exporter has been shown to be lipid-dependent (Becker et al. 2010; Oliveira et al., 2011). The alternating access mechanism and the flippase activity of this ABC exporter has been shown to be lipid-dependent (Immadisetty et al. 2019).