Use of designed metal-binding sites to study helix proximity in the lactose permease of Escherichia coli. 2. Proximity of helix IX (Arg302) with helix X (His322 and Glu325).
about
Evolutionary mix-and-match with MFS transportersAn approach to membrane protein structure without crystals.Alanine insertion scanning mutagenesis of lactose permease transmembrane helices.Second-site suppression of a nonfunctional mutation within the Leishmania donovani inosine-guanosine transporter.Arg-302 facilitates deprotonation of Glu-325 in the transport mechanism of the lactose permease from Escherichiacoli.A chemiosmotic mechanism of symportStructural model for 12-helix transporters belonging to the major facilitator superfamily.Lessons from lactose permeaseConversion of agonist site to metal-ion chelator site in the beta(2)-adrenergic receptor.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.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.Connectivity and orientation of the seven helical bundle in the tachykinin NK-1 receptor probed by zinc site engineering.pKa of Glu325 in LacY.Delineation of an endogenous zinc-binding site in the human dopamine transporter.The role of helix VIII in the lactose permease of Escherichia coli: I. Cys-scanning mutagenesis.Defining proximity relationships in the tertiary structure of the dopamine transporter. Identification of a conserved glutamic acid as a third coordinate in the endogenous Zn(2+)-binding site.Structural topology of transmembrane helix 10 in the lactose permease of Escherichia coli.Function, Structure, and Evolution of the Major Facilitator Superfamily: The LacY Manifesto
P2860
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P2860
Use of designed metal-binding sites to study helix proximity in the lactose permease of Escherichia coli. 2. Proximity of helix IX (Arg302) with helix X (His322 and Glu325).
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
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1995年學術文章
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name
Use of designed metal-binding ...... h helix X (His322 and Glu325).
@en
Use of designed metal-binding ...... coli. 2. Proximity of helix IX
@nl
type
label
Use of designed metal-binding ...... h helix X (His322 and Glu325).
@en
Use of designed metal-binding ...... coli. 2. Proximity of helix IX
@nl
prefLabel
Use of designed metal-binding ...... h helix X (His322 and Glu325).
@en
Use of designed metal-binding ...... coli. 2. Proximity of helix IX
@nl
P356
P1433
P1476
Use of designed metal-binding ...... h helix X (His322 and Glu325).
@en
P2093
P304
15667-15670
P356
10.1021/BI00048A010
P407
P577
1995-12-01T00:00:00Z