Characterization of Glu126 and Arg144, two residues that are indispensable for substrate binding in the lactose permease of Escherichia coli.
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Structural determination of wild-type lactose permeaseStructure of sugar-bound LacYThe kamikaze approach to membrane transportEvolutionary mix-and-match with MFS transportersEvolutionary mix-and-match with MFS transporters IIArg-52 in the melibiose carrier of Escherichia coli is important for cation-coupled sugar transport and participates in an intrahelical salt bridge.Arg-302 facilitates deprotonation of Glu-325 in the transport mechanism of the lactose permease from Escherichiacoli.Second-site suppressor mutations of inactivating substitutions at gly247 of the tetracycline efflux protein, Tet(B).Changing the lactose permease of Escherichia coli into a galactose-specific symporterStructure-function relationships of integral membrane proteins: membrane transporters vs channels.Cysteine-scanning analysis of the nucleobase-ascorbate transporter signature motif in YgfO permease of Escherichia coli: Gln-324 and Asn-325 are essential, and Ile-329-Val-339 form an alpha-helix.A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrESugar binding and protein conformational changes in lactose permeaseToward the bilayer proteome, electrospray ionization-mass spectrometry of large, intact transmembrane proteinsConformational flexibility at the substrate binding site in the lactose permease of Escherichia coli.Structure of LacY with an α-substituted galactoside: Connecting the binding site to the protonation site.Role of the irreplaceable residues in the LacY alternating access mechanismLessons from lactose permeaseExploiting luminescence spectroscopy to elucidate the interaction between sugar and a tryptophan residue in the lactose permease of Escherichia coli.Unraveling the mechanism of the lactose permease of Escherichia coli.Binding affinity of lactose permease is not altered by the H+ electrochemical gradient.The periplasmic cavity of LacY mutant Cys154→Gly: how open is open?Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY.Residues in the H+ translocation site define the pKa for sugar binding to LacY.Galactoside-binding site in LacY.Identification of essential charged residues in transmembrane segments of the multidrug transporter MexB of Pseudomonas aeruginosa.An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli.Conservation of residues involved in sugar/H(+) symport by the sucrose permease of Escherichia coli relative to lactose permease.Probing the mechanism of a membrane transport protein with affinity inactivators.In vitro synthesis of lactose permease to probe the mechanism of membrane insertion and folding.Sugar recognition by the lactose permease of Escherichia coli.Function, Structure, and Evolution of the Major Facilitator Superfamily: The LacY Manifesto
P2860
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P2860
Characterization of Glu126 and Arg144, two residues that are indispensable for substrate binding in the lactose permease of Escherichia coli.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Characterization of Glu126 and ...... permease of Escherichia coli.
@en
type
label
Characterization of Glu126 and ...... permease of Escherichia coli.
@en
prefLabel
Characterization of Glu126 and ...... permease of Escherichia coli.
@en
P2093
P356
P1433
P1476
Characterization of Glu126 and ...... permease of Escherichia coli.
@en
P2093
P304
P356
10.1021/BI982200H
P407
P577
1999-01-01T00:00:00Z