The conserved motif, GXXX(D/E)(R/K)XG[X](R/K)(R/K), in hydrophilic loop 2/3 of the lactose permease.

doi:10.1074/jbc.270.27.16251

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Article

The conserved motif, GXXX(D/E)(R/K)XG[X](R/K)(R/K), in hydrophilic loop 2/3 of the lactose permease.

The Journal of biological chemistry - 7 Jul 1995

Jessen-Marshall A E, Paul N J, Brooker R J

Abstract excerpt

A conserved motif, GXXX(D/E)(R/K)XG(R/K)(R/K), has been identified among a large group of evolutionarily related membrane proteins involved in the transport of small molecules across the membrane. To determine the importance of this motif within the lactose permease of Escherichia coli, a total of 28 site-directed mutations at the conserved first, fifth, sixth, eighth, ninth, and tenth positions were analyzed. A...

Topics

Amino Acid Sequence
Base Sequence
Biological Transport
Carrier Proteins
Conserved Sequence
Culture Media
DNA Mutational Analysis
Escherichia coli Proteins
Galactosides
Membrane Transport Proteins
Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Monosaccharide Transport Proteins

Mutagenesis, Site-Directed

Phenotype

Protein Structure, Secondary

Protons

Sequence Homology, Amino Acid

Source

Open in PubMed

Identifiers

PMID: 7608191
DOI: 10.1074/jbc.270.27.16251

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7608191-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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The conserved motif, GXXX(D/E)(R/K)XG[X](R/K)(R/K), in hydrophilic loop 2/3 of the lactose permease.PMID 7608191Read ↗

An analysis of suppressor mutations suggests that the two halves of the lactose permease function in a symmetrical manner.Semantic proximity Read ↗

Evidence that transmembrane segment 2 of the lactose permease is part of a conformationally sensitive interface between the two halves of the protein.Semantic proximity Read ↗

Evidence for structural symmetry and functional asymmetry in the lactose permease of Escherichia coli.Semantic proximity Read ↗

Structural topology of transmembrane helix 10 in the lactose permease of Escherichia coli.Semantic proximity Read ↗

The conserved motif in hydrophilic loop 2/3 and loop 8/9 of the lactose permease of Escherichia coli. Analysis of suppressor mutations.Semantic proximity Read ↗

Suppressor analysis of mutations in the loop 2-3 motif of lactose permease: evidence that glycine-64 is an important residue for conformational changes.Semantic proximity Read ↗

Mutational analysis of putative helix-helix interacting GxxxG-motifs and tryptophan residues in the two-peptide bacteriocin lactococcin G.Semantic proximity Read ↗

A face on transmembrane segment 8 of the lactose permease is important for transport activity.Semantic proximity Read ↗

Identification of essential arginine residues of Escherichia coli DedA/Tvp38 family membrane proteins YqjA and YghB.Semantic proximity Read ↗

The last two cytoplasmic loops in the lactose permease of Escherichia coli comprise a discontinuous epitope for a monoclonal antibody.Semantic proximity Read ↗

Cysteine-scanning mutagenesis of helix II and flanking hydrophilic domains in the lactose permease of Escherichia coli.Semantic proximity Read ↗

Analysis of conserved NCS2 motifs in the Escherichia coli xanthine permease XanQ.Semantic proximity Read ↗

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