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

A pH-gated conformational switch regulates the phosphatase activity of bifunctional HisKA-family histidine kinases.

Nature communications - 13 Dec 2017

Liu Yixiang, Rose Joshua, Huang Shaojia, Hu Yangbo, Wu Qiong, Wang Dan, Li Conggang, Liu Maili, Zhou Pei, Jiang Ling

Abstract excerpt

Histidine kinases are key regulators in the bacterial two-component systems that mediate the cellular response to environmental changes. The vast majority of the sensor histidine kinases belong to the bifunctional HisKA family, displaying both kinase and phosphatase activities toward their substrates. The molecular mechanisms regulating the opposing activities of these enzymes are not well understood. Through a...

Read the complete abstract on PubMed

Topics

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

Share to RAW 264.7 Cells
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Histidine Kinase

Share to Hydrogen-Ion Concentration

Share to Magnetic Resonance Spectroscopy

Share to Phosphoprotein Phosphatases

Share to Salmonella enterica

Share to Thermotoga maritima

Source

Open in PubMed Open full text

Identifiers

PMID: 29235472
DOI: 10.1038/s41467-017-02310-9
PMCID: PMC5727384

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A pH-gated conformational switch regulates the phosphatase activity of bifunctional HisKA-family histidine kinases.PMID 29235472Read ↗

Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases.Semantic proximity Read ↗

Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein.Semantic proximity Read ↗

Structural insights into the signal transduction mechanism of the K+-sensing two-component system KdpDE.Semantic proximity Read ↗

Switching Protein Conformational Substates by Protonation and Mutation.Semantic proximity Read ↗

Helix bundle loops determine whether histidine kinases autophosphorylate in cis or in trans.Semantic proximity Read ↗

The histidine phosphatase superfamily: structure and functionSemantic proximity Read ↗

YmoA functions as a molecular stress sensor in <i>Yersinia</i>Semantic proximity Read ↗

A TPR scaffold couples signal detection to OdhI phosphorylation in metabolic control by the protein kinase PknGSemantic proximity Read ↗

<i>In situ</i> NMR reveals a pH sensor motif in an outer membrane protein that drives bacterial vesicle productionSemantic proximity Read ↗

The SixA phospho-histidine phosphatase modulates the ArcB phosphorelay signal transduction in Escherichia coli.Semantic proximity Read ↗

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

High-throughput discovery of peptide activators of a bacterial sensor kinaseSemantic proximity Read ↗

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