An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli.
about
X-ray structure of EmrE supports dual topology model.A glutamate switch controls voltage-sensitive phosphatase functionYeast Fex1p Is a Constitutively Expressed Fluoride Channel with Functional Asymmetry of Its Two Homologous DomainsFunctional analysis of novel multidrug transporters from human pathogensProtonation of a glutamate residue modulates the dynamics of the drug transporter EmrECompetition as a way of life for H(+)-coupled antiportersIntrinsic conformational plasticity of native EmrE provides a pathway for multidrug resistanceA structured loop modulates coupling between the substrate-binding and dimerization domains in the multidrug resistance transporter EmrE.Interaction of transported drugs with the lipid bilayer and P-glycoprotein through a solvation exchange mechanism.Acidic residues in the lactococcal multidrug efflux pump LmrP play critical roles in transport of lipophilic cationic compounds.Structure-function studies of the SLC17 transporter sialin identify crucial residues and substrate-induced conformational changesA common binding site for substrates and protons in EmrE, an ion-coupled multidrug transporter.Structure, dynamics, and substrate-induced conformational changes of the multidrug transporter EmrE in liposomes.The drug/metabolite transporter superfamily.Amino acid residues essential for function of the MexF efflux pump protein of Pseudomonas aeruginosaCrosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer.A structural model of EmrE, a multi-drug transporter from Escherichia coli.Structure of the multidrug resistance efflux transporter EmrE from Escherichia coliThe projection structure of EmrE, a proton-linked multidrug transporter from Escherichia coli, at 7 A resolutionA membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrEMystery of multidrug transporters: the answer can be simple.Role of glutamate residues in substrate recognition by human MATE1 polyspecific H+/organic cation exporter.Structure and function of efflux pumps that confer resistance to drugsThe fast release of sticky protons: kinetics of substrate binding and proton release in a multidrug transporterIn vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric stateAsymmetric protonation of EmrE.Small multidrug resistance protein EmrE reduces host pH and osmotic tolerance to metabolic quaternary cation osmoprotectants.New substrates on the block: clinically relevant resistances for EmrE and homologues.Promiscuity in multidrug recognition and transport: the bacterial MFS Mdr transporters.An emerging consensus for the structure of EmrE.NMR and EPR studies of membrane transporters.Structural and mechanistic diversity of multidrug transporters.Analysis of the topology of Vibrio cholerae NorM and identification of amino acid residues involved in norfloxacin resistance.Identification of a glycine motif required for packing in EmrE, a multidrug transporter from Escherichia coli.Identification of essential charged residues in transmembrane segments of the multidrug transporter MexB of Pseudomonas aeruginosa.Overexpression of the Escherichia coli sugE gene confers resistance to a narrow range of quaternary ammonium compounds.Membrane topology of the multidrug transporter MdfA: complementary gene fusion studies reveal a nonessential C-terminal domain.A novel mechanism for fine-tuning open-state stability in a voltage-gated potassium channel.Amino acid composition analysis of secondary transport proteins from Escherichia coli with relation to functional classification, ligand specificity and structure.In vitro membrane protein synthesis inside Sec translocon-reconstituted cell-sized liposomes.
P2860
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P2860
An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli.
@en
An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli.
@nl
type
label
An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli.
@en
An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli.
@nl
prefLabel
An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli.
@en
An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli.
@nl
P2860
P356
P1476
An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli.
@en
P2093
H Yerushalmi
P2860
P304
P356
10.1074/JBC.275.8.5264
P407
P577
2000-02-01T00:00:00Z