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

Structure-function analysis of the vitamin B12 receptor of Escherichia coli by means of informational suppression.

Molecular microbiology - 1 Jan 1995

Hufton S E, Ward R J, Bunce N A, Armstrong J T, Fletcher A J, Glass R E

Abstract excerpt

We describe a genetic analysis of the vitamin B12 receptor of Escherichia coli. Through the use of informational suppression, we have been able to generate a family of receptor variants, each identical save for a single, known substitution (Ser, Gln, Lys, Tyr, Leu, Cys, Phe) at a known site. We have studied 22 different mutants, 14 in detail, distributed throughout the length of the btuB gene. Most amino acid...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Bacterial Proteins

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

Share to Escherichia coli

Share to Genes, Bacterial

Share to Membrane Proteins

Share to Molecular Sequence Data

Share to Phenotype

Share to Protein Conformation

Source

Identifiers

PMID: 7746157
DOI: 10.1111/j.1365-2958.1995.tb02251.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

Structure-function analysis of the vitamin B12 receptor of Escherichia coli by means of informational suppression.PMID 7746157Read ↗

Mapping the functional landscape of the receptor binding domain of T7 bacteriophage by deep mutational scanning.Semantic proximity Read ↗

Temperature-sensitive suppressor mutations of the Escherichia coli DNA gyrase B protein.Semantic proximity Read ↗

Complete alanine scanning of the Escherichia coli RbsB ribose binding protein reveals residues important for chemoreceptor signaling and periplasmic abundance.Semantic proximity Read ↗

Multiple extracellular loops contribute to substrate binding and transport by the Escherichia coli cobalamin transporter BtuB.Semantic proximity Read ↗

Molecular characterization of the Enterobacter aerogenes tonB gene: identification of a novel type of tonB box suppressor mutant.Semantic proximity Read ↗

Characterisation of a natural variant of the γ-butyrolactone signalling receptor.Semantic proximity Read ↗

The TolC protein of Escherichia coli serves as a cell-surface receptor for the newly characterized TLS bacteriophage.Semantic proximity Read ↗

Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli.Semantic proximity Read ↗

Mutations in the Escherichia coli receptor FepA reveal residues involved in ligand binding and transport.Semantic proximity Read ↗

Molecular analysis of the Escherichia coli ferric enterobactin receptor FepA.Semantic proximity Read ↗

Escherichia coli TolA tolerates multiple amino-acid substitutions as revealed by screening randomized variants for membrane integrity and phage receptor function.Semantic proximity Read ↗

Mutational Analysis of Binding Protein-Chemoreceptor Interactions.Semantic proximity Read ↗

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