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-scanning analysis of the dimerization domain of EnvZ, an osmosensing histidine kinase.

Journal of bacteriology - 1 Jun 2003

Qin Ling, Cai Shengjian, Zhu Yan, Inouye Masayori

Abstract excerpt

EnvZ and OmpR are a transmembrane sensor and its cognate response regulator, respectively, regulating the transcription of porin genes in response to medium osmolarity in Escherichia coli. The cytoplasmic domain of EnvZ (EnvZc) possesses both kinase and phosphatase activities and can be dissected into two functional domains, A and B. Here, we performed a cysteine-scanning analysis of domain A, a 67-residue...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Outer Membrane Proteins
Share to Culture Media
Share to Cysteine

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

Share to Dimerization

Share to Histidine Kinase

Share to Multienzyme Complexes

Share to Osmolar Concentration

Share to Phosphoric Monoester Hydrolases

Source

Open in PubMed Open full text

Identifiers

PMID: 12754242
DOI: 10.1128/JB.185.11.3429-3435.2003
PMCID: PMC155382

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-scanning analysis of the dimerization domain of EnvZ, an osmosensing histidine kinase.PMID 12754242Read ↗

Mutations that alter the kinase and phosphatase activities of the two-component sensor EnvZ.Semantic proximity Read ↗

Transmembrane signal transduction and osmoregulation in Escherichia coli: functional importance of the transmembrane regions of membrane-located protein kinase, EnvZ.Semantic proximity Read ↗

Phosphatase activity of histidine kinase EnvZ without kinase catalytic domain.Semantic proximity Read ↗

The role of the G2 box, a conserved motif in the histidine kinase superfamily, in modulating the function of EnvZ.Semantic proximity Read ↗

Kinase activity of EnvZ, an osmoregulatory signal transducing protein of Escherichia coli.Semantic proximity Read ↗

The inner membrane histidine kinase EnvZ senses osmolality via helix-coil transitions in the cytoplasm.Semantic proximity Read ↗

Role of His243 in the phosphatase activity of EnvZ in Escherichia coli.Semantic proximity Read ↗

A single amino acid substitution in the C terminus of OmpR alters DNA recognition and phosphorylation.Semantic proximity Read ↗

Transmembrane signal transduction and osmoregulation in Escherichia coli: I. Analysis by site-directed mutagenesis of the amino acid residues involved in phosphotransfer between the two regulatory components, EnvZ and OmpR.Semantic proximity Read ↗

Re-examination of the role of the periplasmic domain of EnvZ in sensing of osmolarity signals in Escherichia coli.Semantic proximity Read ↗

A phosphorylation site mutant of OmpR reveals different binding conformations at ompF and ompC.Semantic proximity Read ↗

Intramolecular second-site revertants to the phosphorylation site mutation in OmpR, a kinase-dependent transcriptional activator in Escherichia coli.Semantic proximity Read ↗

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