Cysteine 148 in the lactose permease of Escherichia coli is a component of a substrate binding site. 1. Site-directed mutagenesis studies.
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Structural determination of wild-type lactose permeaseThe kamikaze approach to membrane transportTopology of allosteric regulation of lactose permeaseHelix packing of lactose permease in Escherichia coli studied by site-directed chemical cleavage.Identification of a membrane-localized cysteine cluster near the substrate-binding sites of the Streptococcus equisimilis hyaluronan synthaseChanging the lactose permease of Escherichia coli into a galactose-specific symporterStructure-function relationships of integral membrane proteins: membrane transporters vs channels.Thiol modification of cysteine 327 in the eighth transmembrane domain of the light subunit xCT of the heteromeric cystine/glutamate antiporter suggests close proximity to the substrate binding site/permeation pathway.Conformational flexibility at the substrate binding site in the lactose permease of Escherichia coli.The substrate-binding site in the lactose permease of Escherichia coli.Lessons from lactose permeaseProton-dependent multidrug efflux systems.A general method for determining helix packing in membrane proteins in situ: helices I and II are close to helix VII in the lactose permease of Escherichia coli.Unraveling the mechanism of the lactose permease of Escherichia coli.Site-directed spin labeling and chemical crosslinking demonstrate that helix V is close to helices VII and VIII in the lactose permease of Escherichia coli.The periplasmic cavity of LacY mutant Cys154→Gly: how open is open?Elucidation of substrate binding interactions in a membrane transport protein by mass spectrometry.Cysteine 144 in the third transmembrane domain of the creatine transporter is located close to a substrate-binding site.The role of helix VIII in the lactose permease of Escherichia coli: II. Site-directed sulfhydryl modification.Evidence for phospholipid microdomain formation in liquid crystalline liposomes reconstituted with Escherichia coli lactose permease.The role of transmembrane domain III in the lactose permease of Escherichia coliThe role of helix VIII in the lactose permease of Escherichia coli: I. Cys-scanning mutagenesis.Probing the mechanism of a membrane transport protein with affinity inactivators.In vitro folding of a membrane protein: effect of denaturation and renaturation on substrate binding by the lactose permease of Escherichia coli.Cys(577) is a conformationally mobile residue in the ATP-binding domain of the Na,K-ATPase alpha-subunit.Function, Structure, and Evolution of the Major Facilitator Superfamily: The LacY Manifesto
P2860
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P2860
Cysteine 148 in the lactose permease of Escherichia coli is a component of a substrate binding site. 1. Site-directed mutagenesis studies.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Cysteine 148 in the lactose pe ...... -directed mutagenesis studies.
@en
type
label
Cysteine 148 in the lactose pe ...... -directed mutagenesis studies.
@en
prefLabel
Cysteine 148 in the lactose pe ...... -directed mutagenesis studies.
@en
P356
P1433
P1476
Cysteine 148 in the lactose pe ...... -directed mutagenesis studies.
@en
P304
12160-12165
P356
10.1021/BI00206A019
P407
P577
1994-10-01T00:00:00Z