NDLI: Proton motive force mediates a reorientation of the cytosolic domains of the multidrug transporter LmrP

Content Provider	Springer Nature Link
Author	Gbaguidi, B. Mazurkiewicz, P. Konings, W. N. Driessen, A. J. M. Ruysschaert, J. M. Viga, C.
Copyright Year	2004
Abstract	LmrP from Lactococcus lactis is a 45-kDa membrane protein that confers resistance to a wide variety of lipophilic compounds by acting as a proton motive force-driven efflux pump. This study shows that both the proton motive force and ligand interaction alter the accessibility of cytosolic tryptophan residues to a hydrophilic quencher. The proton motive force mediates an increase of LmrP accessibility toward the external medium and results in higher drug binding. Residues Asp128 and Asp68, from cytosolic loops, are involved in the proton motive force-mediated accessibility change. Ligand binding does not modify the protein accessibility, but the proton motive force-mediated restructuring is prerequisite for a subsequent accessibility change mediated by ligand binding. Asp142 cooperates with other membrane-embedded carboxylic residues to promote a conformational change that increases LmrP accessibility toward: the hydrophilic quencher. This drug binding-mediated reorganization may be related to the transition between the high- and low-affinity drug-binding sites and is crucial for drug release in the extracellular medium.
Starting Page	2646
Ending Page	2657
Page Count	12
File Format	PDF
ISSN	1420682X
Journal	Cellular and Molecular Life Sciences
Volume Number	61
Issue Number	19
e-ISSN	14209071
Language	English
Publisher	Birkhäuser-Verlag
Publisher Date	2004-01-01
Publisher Place	Basel
Access Restriction	Subscribed
Subject Keyword	Accessibility change LmrP multidrug resistance proton motive force Biomedicine general Life Sciences Biochemistry Cell Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology Molecular Medicine Pharmacology Cellular and Molecular Neuroscience

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