Lipid composition regulates the orientation of transmembrane helices in HorA, an ABC multidrug transporter

Journal of Biological Chemistry

Volumn 285, Issue 19, 2010, Pages 14144-14151

  Gustot, Adelin ^a   Smriti, ^b   Ruysschaert, Jean Marie ^a   Mchaourab, Hassane ^b   Govaerts, Cédric ^a  

^a UNIVERSITÉ LIBRE DE BRUXELLES   (Belgium)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ATP HYDROLYSIS; ATP-ASE ACTIVITY; ATP-BINDING CASSETTE TRANSPORTERS; ATR FTIR; ATTENUATED TOTAL REFLECTIONS; BACKBONE CARBONYL; BACTERIAL MEMBRANES; BI-LAYER; ELECTRON PARAMAGNETIC RESONANCE; HYDROGEN/DEUTERIUM EXCHANGE; LARGE CLASS; LIPID COMPOSITION; LIPID PHASE; MOLECULAR PUMPS; MULTIDRUG TRANSPORTERS; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOLAMINE; SECONDARY STRUCTURES; SPIN LABEL; STRUCTURAL CHANGE; TRANSMEMBRANE HELICES;

BACTERIOLOGY; CHEMOTHERAPY; ELECTRON SPIN RESONANCE SPECTROSCOPY; FOURIER TRANSFORM INFRARED SPECTROSCOPY; LIPOSOMES; PARAMAGNETIC RESONANCE; PHOSPHOLIPIDS; POLYVINYL ALCOHOLS; SUBSTRATES;

MOLECULAR OXYGEN;

ABC TRANSPORTER; ADENOSINE TRIPHOSPHATE; CARBONYL DERIVATIVE; CYSTEINE; GLYCOPROTEIN P; HOE 33342; HORA PROTEIN; LIPOSOME; OXYGEN; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOLAMINE; SOLVENT; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL MEMBRANE; BILAYER MEMBRANE; CONTROLLED STUDY; DEUTERIUM HYDROGEN EXCHANGE; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; HYDROLYSIS; INFRARED SPECTROSCOPY; LACTOBACILLUS BREVIS; LIPID COMPOSITION; LIPID MEMBRANE; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SPIN LABELING;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; ATP-BINDING CASSETTE TRANSPORTERS; BIOLOGICAL TRANSPORT; CIRCULAR DICHROISM; ELECTRON SPIN RESONANCE SPECTROSCOPY; LACTOBACILLUS; LIPID BILAYERS; LIPOSOMES; MOLECULAR SEQUENCE DATA; PHOSPHATIDYLCHOLINES; PHOSPHATIDYLETHANOLAMINES; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

BACTERIA (MICROORGANISMS);

EID: 77952003799     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.079673     Document Type: Article

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