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

Maltose-binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor.

Molecular microbiology - 1 Mar 1997

Gardina P J, Bormans A F, Hawkins M A, Meeker J W, Manson M D

Abstract excerpt

The Tar chemotactic signal transducer of Escherichia coli mediates attractant responses to L-aspartate and to maltose. Aspartate binds across the subunit interface of the periplasmic receptor domain of a Tar homodimer. Maltose, in contrast, first binds to the periplasmic maltose-binding protein (MBP), which in its ligand-stabilized closed form then interacts with Tar. Intragenic complementation was used to...

Read the complete abstract on PubMed

Topics

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

Share to Alleles
Share to Bacterial Proteins
Share to DNA Mutational Analysis

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

Share to Escherichia coli

Share to Gene Expression

Share to Genes, Bacterial

Share to Genetic Complementation Test

Share to Membrane Proteins

Source

Identifiers

PMID: 9106209
DOI: 10.1046/j.1365-2958.1997.3001661.x

Genes

MBP

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

Maltose-binding protein interacts simultaneously and asymmetrically with both subunits of the Tar chemoreceptor.PMID 9106209Read ↗

Signaling by the Escherichia coli aspartate chemoreceptor Tar with a single cytoplasmic domain per dimer.Semantic proximity Read ↗

Attractant signaling by an aspartate chemoreceptor dimer with a single cytoplasmic domain.Semantic proximity Read ↗

Maltose-binding protein containing an interdomain disulfide bridge confers a dominant-negative phenotype for transport and chemotaxis.Semantic proximity Read ↗

Progress in the identification of interaction sites on the periplasmic maltose binding protein from E coli.Semantic proximity Read ↗

Conformational suppression of inter-receptor signaling defects.Semantic proximity Read ↗

Role of threonine residue 154 in ligand recognition of the tar chemoreceptor in Escherichia coli.Semantic proximity Read ↗

Arginine mutations within a transmembrane domain of Tar, an Escherichia coli aspartate receptor, can drive homodimer dissociation and heterodimer association in vivo.Semantic proximity Read ↗

Two domains of MalT, the activator of the Escherichia coli maltose regulon, bear determinants essential for anti-activation by MalK.Semantic proximity Read ↗

Transmembrane signalling by the chimeric chemosensory receptors of Escherichia coli Tsr and Tar with heterologous membrane-spanning regions.Semantic proximity Read ↗

Escherichia coli tatC mutations that suppress defective twin-arginine transporter signal peptides.Semantic proximity Read ↗

Genetically probing the regions of ribose-binding protein involved in permease interaction.Semantic proximity Read ↗

Escherichia coli tat mutant strains are able to transport maltose in the absence of an active malE gene.Semantic proximity Read ↗

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