A new experimental approach to detect long-range conformational changes transmitted between the membrane and cytosolic domains of LmrA, a bacterial multidrug transporter

FEBS Letters

Volumn 530, Issue 1-3, 2002, Pages 197-203

  Vigano, Catherine ^a   Grimard, Vinciane ^a   Margolles, Abelardo ^b   Goormaghtigh, Erik ^a   Van Veen, Hendrik W ^c   Konings, Wil N ^b   Ruysschaert, Jean Marie ^a  

^a UNIVERSITÉ LIBRE DE BRUXELLES   (Belgium)

^b UNIVERSITY OF GRONINGEN   (Netherlands)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Conformational change; Infrared spectroscopy; LmrA; Membrane domain; Multidrug resistance; Tryptophan fluorescence

Indexed keywords

ADENOSINE TRIPHOSPHATE; CARRIER PROTEIN; MEMBRANE PROTEIN; NUCLEOTIDE; PROTEIN LMRA; UNCLASSIFIED DRUG; WATER;

ANTIBIOTIC RESISTANCE; ARTICLE; ATTENUATION; BACTERIAL MEMBRANE; CONTROLLED STUDY; CYTOSOL; DRUG TRANSPORT; FLUORESCENCE; HYDROLYSIS; INFRARED RADIATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN HYDROLYSIS; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION; SOLUBILITY;

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; CATALYSIS; CELL MEMBRANE; CYTOSOL; DRUG RESISTANCE, MICROBIAL; HYDROLYSIS; LACTOCOCCUS LACTIS; MULTIDRUG RESISTANCE-ASSOCIATED PROTEINS; PROTEIN CONFORMATION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

BACTERIA (MICROORGANISMS); LACTOCOCCUS LACTIS;

EID: 0037163877     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(02)03485-3     Document Type: Article

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