The conformational transition pathway of ATP binding cassette transporter MsbA revealed by atomistic simulations.

ABSTRACT: ATP binding cassette transporters are integral membrane proteins that use the energy released from ATP hydrolysis at the two nucleotide binding domains (NBDs) to translocate a wide variety of substrates through a channel at the two transmembrane domains (TMDs) across the cell membranes. MsbA from Gram-negative bacteria is a lipid and multidrug resistance ATP binding cassette exporter that can undergo large scale conformational changes between the outward-facing and the inward-facing conformations revealed by crystal structures in different states. Here, we use targeted molecular dynamics simulation methods to explore the atomic details of the conformational transition from the outward-facing to the inward-facing states of MsbA. The molecular dynamics trajectories revealed a clear spatiotem

SUBMITTER: Weng JW 

PROVIDER: S-EPMC2823423 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature