Abstract
The molecular dynamics of the 64 kDa ABC multidrug efflux pump LmrA from Lactococcus lactis within lipid membranes has been investigated by deuterium solid-state NMR. Deuteriomethyl-labeled alanine has been used to probe global protein backbone dynamics. A comparison of static deuterium NMR spectra of full-length LmrA in the resting state and its isolated transmembrane domain revealed a high mobility for the nucleotide binding domains. Their motional freedom is restricted upon ATP binding as seen for LmrA in complex with AMP-PNP, a nonhydrolyzable ATP analogue. LmrA returns to full motional flexibility in the posthydrolysis, vanadate-trapped state. These experiments provide insight into the molecular dynamics of a full-length ABC transporter during the catalytic cycle. Data are discussed in the context of known biochemical data and structural models of ABC transporters.
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