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

Identification of the dimer interface of the lactose transport protein from Streptococcus thermophilus.

Journal of molecular biology - 3 Oct 2003

Geertsma Eric R, Duurkens Ria H, Poolman Bert

Abstract excerpt

The lactose transporter from Streptococcus thermophilus catalyses the symport of galactosides and protons. The carrier domain of the protein harbours the contact sites for dimerization, and the individual subunits in the dimer interact functionally during the transport reaction. As a first step towards the elucidation of the mechanism behind the cooperation between the subunits, regions involved in the dimer...

Read the complete abstract on PubMed

Topics

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

Share to Cross-Linking Reagents
Share to Detergents
Share to Ethylmaleimide

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Monosaccharide Transport Proteins

Share to Protein Structure, Quaternary

Share to Protons

Share to Streptococcus

Share to Symporters

Source

Identifiers

PMID: 14499618
DOI: 10.1016/j.jmb.2003.07.010

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of the dimer interface of the lactose transport protein from Streptococcus thermophilus.PMID 14499618Read ↗

Functional interactions between the subunits of the lactose transporter from Streptococcus thermophilus.Semantic proximity Read ↗

Helix packing in the lactose permease of Escherichia coli: localization of helix VI.Semantic proximity Read ↗

An early event in the transport mechanism of LacY protein: interaction between helices V and I.Semantic proximity Read ↗

Probing interactions of the Escherichia coli F0F1 ATP synthase beta and gamma subunits with disulphide cross-links.Semantic proximity Read ↗

Targeted disulfide cross-linking of the MotB protein of Escherichia coli: evidence for two H(+) channels in the stator Complex.Semantic proximity Read ↗

Disulfide bond formation in periplasm of Escherichia coli.Semantic proximity Read ↗

Helices VII and X in the lactose permease of Escherichia coli: proximity and ligand-induced distance changes.Semantic proximity Read ↗

Dimerisation mutants of Lac repressor. II. A single amino acid substitution, D278L, changes the specificity of dimerisation.Semantic proximity Read ↗

Membrane binding modulates the quaternary structure of CTP:phosphocholine cytidylyltransferase.Semantic proximity Read ↗

Opsin is present as dimers in COS1 cells: identification of amino acids at the dimeric interface.Semantic proximity Read ↗

Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit beta-strand alignment.Semantic proximity Read ↗

The biological assembly of OXA-48 reveals a dimer interface with high charge complementarity and very high affinity.Semantic proximity Read ↗

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