A single negatively charged residue affects the orientation of a membrane protein in the inner membrane of Escherichia coli only when it is located adjacent to a transmembrane domain.
about
Topological mapping methods for α-helical bacterial membrane proteins--an update and a guideLipids in the assembly of membrane proteins and organization of protein supercomplexes: implications for lipid-linked disordersTopological analysis of a haloacid permease of a Burkholderia sp. bacterium with a PhoA-LacZ reporter.Lipids and topological rules governing membrane protein assembly.Phosphatidylethanolamine and monoglucosyldiacylglycerol are interchangeable in supporting topogenesis and function of the polytopic membrane protein lactose permease.Transmembrane protein topology mapping by the substituted cysteine accessibility method (SCAM(TM)): application to lipid-specific membrane protein topogenesisDiversity and versatility of lipid-protein interactions revealed by molecular genetic approaches.A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition.Lipid-dependent membrane protein topogenesis.Charge requirements of lipid II flippase activity in Escherichia coliLipids and topological rules of membrane protein assembly: balance between long and short range lipid-protein interactions.Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.To flip or not to flip: lipid-protein charge interactions are a determinant of final membrane protein topology.Identification of protein functions using a machine-learning approach based on sequence-derived properties.Lipid-protein interactions drive membrane protein topogenesis in accordance with the positive inside rule.Charged residues next to transmembrane regions revisited: "Positive-inside rule" is complemented by the "negative inside depletion/outside enrichment rule"Characterization and mutational analysis of three allelic lsc genes encoding levansucrase in Pseudomonas syringae.Reversible topological organization within a polytopic membrane protein is governed by a change in membrane phospholipid composition.Phospholipids as determinants of membrane protein topology. Phosphatidylethanolamine is required for the proper topological organization of the gamma-aminobutyric acid permease (GabP) of Escherichia coli.Effects of mixed proximal and distal topogenic signals on the topological sensitivity of a membrane protein to the lipid environment.
P2860
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P2860
A single negatively charged residue affects the orientation of a membrane protein in the inner membrane of Escherichia coli only when it is located adjacent to a transmembrane domain.
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
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-hant
name
A single negatively charged re ...... ent to a transmembrane domain.
@en
A single negatively charged re ...... ent to a transmembrane domain.
@nl
type
label
A single negatively charged re ...... ent to a transmembrane domain.
@en
A single negatively charged re ...... ent to a transmembrane domain.
@nl
prefLabel
A single negatively charged re ...... ent to a transmembrane domain.
@en
A single negatively charged re ...... ent to a transmembrane domain.
@nl
P2093
P2860
P356
P1476
A single negatively charged re ...... ent to a transmembrane domain.
@en
P2093
P2860
P304
33757-33763
P356
10.1074/JBC.274.47.33757
P407
P577
1999-11-01T00:00:00Z