Abstract
The multidrug and toxic compound extrusion (MATE) transporters expel chemical compounds out of the cell which results in multidrug resistance. Recently, a distinct conformation of the inward-facing crystal structures for DinF protein from Pyrococcus furiosus (PfMATE) has been determined [Zakrzewska et al. (1)]. This has allowed investigations of the mechanisms of conformational transitions between inward- and outward-facing structures of the PfMATE. We performed molecular dynamics simulations of the inward-facing (IF) and the outward-facing (OF) PfMATE in the native archaeal lipid bilayer to investigate the atomistic level details of the conformational changes.
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