Dynamics of alpha-helical subdomain rotation in the intact maltose ATP-binding cassette transporter.

ABSTRACT: ATP-binding cassette (ABC) transporters are powered by a nucleotide-binding domain dimer that opens and closes during cycles of ATP hydrolysis. These domains consist of a RecA-like subdomain and an α-helical subdomain that is specific to the family. Many studies on isolated domains suggest that the helical subdomain rotates toward the RecA-like subdomain in response to ATP binding, moving the family signature motif into a favorable position to interact with the nucleotide across the dimer interface. Moreover, the transmembrane domains are docked into a cleft at the interface between these subdomains, suggesting a putative role of the rotation in interdomain communication. Electron paramagnetic resonance spectroscopy was used to study the dynamics of this rotation in the intact Escherichia

SUBMITTER: Orelle C 

PROVIDER: S-EPMC2996640 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature