Interactions between phosphatidylethanolamine headgroup and LmrP, a multidrug transporter: A conserved mechanism for proton gradient sensing?

Journal of Biological Chemistry

Volumn 283, Issue 14, 2008, Pages 9369-9376

  Hakizimana, Pierre ^a   Masureel, Matthieu ^a   Gbaguidi, Bénédicte ^a   Ruysschaert, Jean Marie ^a   Govaerts, Cédric ^a  

^a UNIVERSITÉ LIBRE DE BRUXELLES   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ENERGY TRANSFER; HYDROGEN; HYDROGEN BONDS; PHOSPHOLIPIDS; PROBABILITY DENSITY FUNCTION; PROTEINS; PROTONS;

BI LAYERS; BIO-CHEMICALS; BIOPHYSICAL EFFECTS; BIOPHYSICAL PROPERTIES; BULK PROPERTIES; GENERAL FEATURES; HEAD GROUPS; HYDROGEN BONDINGS; LIPID SPECIES; MAJOR FACILITATOR SUPERFAMILIES; MEMBRANE PROTEINS; MULTIDRUG TRANSPORTERS; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOL AMINES; PHOSPHATIDYLETHANOLAMINE; PROTON GRADIENTS; RECONSTITUTED PROTEINS; SINGLE POINTS; SUBSTRATE BINDINGS; TRANSPORT ACTIVITIES; TRYPTOPHAN RESIDUES; UNDERLYING MECHANISMS;

FLOW INTERACTIONS;

ASPARTIC ACID; EMRD PROTEIN; GLYCOPROTEIN P; HYDROGEN; LACY PROTEIN; LIPID; LMRP PROTEIN; METHYL GROUP; PHOSPHATIDYLETHANOLAMINE; PHOSPHOLIPID; PROTEIN DERIVATIVE; PROTON; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CARRIER PROTEIN; LMRP PROTEIN, LACTOCOCCUS LACTIS; PHOSPHATIDYLCHOLINE;

ARTICLE; BIOCHEMISTRY; BIOPHYSICS; CONTROLLED STUDY; ENERGY TRANSFER; HYDROGEN BOND; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN STRUCTURE; AMINO ACID SUBSTITUTION; CHEMISTRY; GENETICS; LACTOCOCCUS LACTIS; LIPID BILAYER; METABOLISM; PHYSIOLOGY; PROTON MOTIVE FORCE; STRUCTURE ACTIVITY RELATION; TRANSPORT AT THE CELLULAR LEVEL;

AMINO ACID MOTIFS; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BIOLOGICAL TRANSPORT; HYDROGEN BONDING; LACTOCOCCUS LACTIS; LIPID BILAYERS; MEMBRANE TRANSPORT PROTEINS; PHOSPHATIDYLCHOLINES; POINT MUTATION; PROTON-MOTIVE FORCE; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 44049083041     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M708427200     Document Type: Article

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