Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Cysteine substitutions for individual residues in helix VI of the melibiose carrier of Escherichia coli.

The Journal of membrane biology - 1 Sept 2001

Ding P Z, Weissborn A C, Wilson T H

Abstract excerpt

The melibiose carrier of Escherichia coli is a cytoplasmic membrane protein that mediates the cotransport of galactosides with H(+), Na(+), or Li(+). In this study we used cysteine-scanning mutagenesis to try to gain information about the position of transmembrane helix VI in the three-dimensional structure of the melibiose carrier. We constructed 23 individual cysteine substitutions in helix VI and an adjacent...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Membrane Proteins
Share to Amino Acid Sequence
Share to Amino Acid Substitution

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cations

Share to Cysteine

Share to Escherichia coli

Share to Mutagenesis, Site-Directed

Share to Symporters

Source

Identifiers

PMID: 11547350
DOI: 10.1007/s00232-001-0053-x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cysteine substitutions for individual residues in helix VI of the melibiose carrier of Escherichia coli.PMID 11547350Read ↗

The melibiose carrier of Escherichia coli: cysteine substitutions for individual residues in helix XI.Semantic proximity Read ↗

An investigation of cysteine mutants on the cytoplasmic loop X/XI in the melibiose transporter of Escherichia coli by using thiol reagents: implication of structural conservation of charged residues.Semantic proximity Read ↗

Physiological evidence for an interaction between helix XI and helices I, II, and V in the melibiose carrier of Escherichia coli.Semantic proximity Read ↗

Physiological evidence for an interaction between helices II and XI in the melibiose carrier of Escherichia coli.Semantic proximity Read ↗

The proximity between helix I and helix XI in the melibiose carrier of Escherichia coli as determined by cross-linking.Semantic proximity Read ↗

Membrane topology of the H+-pyrophosphatase of Streptomyces coelicolor determined by cysteine-scanning mutagenesis.Semantic proximity Read ↗

Sugar recognition mutants of the melibiose carrier of Escherichia coli: possible structural information concerning the arrangement of membrane-bound helices and sugar/cation recognition site.Semantic proximity Read ↗

Alteration of sugar-induced conformational changes of the melibiose permease by mutating Arg141 in loop 4-5.Semantic proximity Read ↗

Evidence for a close association between helix IV and helix XI in the melibiose carrier of Escherichia coli.Semantic proximity Read ↗

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

Alteration of Na(+)-coupled transport in site-directed mutants of the melibiose carrier of Escherichia coli.Semantic proximity Read ↗

Arg-52 in the melibiose carrier of Escherichia coli is important for cation-coupled sugar transport and participates in an intrahelical salt bridge.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.