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

Structures of KaiC circadian clock mutant proteins: a new phosphorylation site at T426 and mechanisms of kinase, ATPase and phosphatase.

PloS one - 26 Nov 2009

Pattanayek Rekha, Mori Tetsuya, Xu Yao, Pattanayek Sabuj, Johnson Carl H, Egli Martin

Abstract excerpt

BACKGROUND: The circadian clock of the cyanobacterium Synechococcus elongatus can be reconstituted in vitro by three proteins, KaiA, KaiB and KaiC. Homo-hexameric KaiC displays kinase, phosphatase and ATPase activities; KaiA enhances KaiC phosphorylation and KaiB antagonizes KaiA. Phosphorylation and dephosphorylation of the two known sites in the C-terminal half of KaiC subunits, T432 and S431, follow a strict...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to Adenosine Triphosphate

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

Share to Bacterial Proteins

Share to Binding Sites

Share to Gene Expression Regulation, Bacterial

Share to Models, Biological

Share to Mutation

Share to Phosphorylation

Source

Open in PubMed Open full text

Identifiers

PMID: 19956664
DOI: 10.1371/journal.pone.0007529
PMCID: PMC2777353

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

Structures of KaiC circadian clock mutant proteins: a new phosphorylation site at T426 and mechanisms of kinase, ATPase and phosphatase.PMID 19956664Read ↗

Dephosphorylation of the core clock protein KaiC in the cyanobacterial KaiABC circadian oscillator proceeds via an ATP synthase mechanism.Semantic proximity Read ↗

Analysis of KaiA-KaiC protein interactions in the cyano-bacterial circadian clock using hybrid structural methods.Semantic proximity Read ↗

Loop-loop interactions regulate KaiA-stimulated KaiC phosphorylation in the cyanobacterial KaiABC circadian clock.Semantic proximity Read ↗

Protein-Protein Interactions in the Cyanobacterial Circadian Clock: Structure of KaiA Dimer in Complex with C-Terminal KaiC Peptides at 2.8 Å Resolution.Semantic proximity Read ↗

Intramolecular regulation of phosphorylation status of the circadian clock protein KaiC.Semantic proximity Read ↗

Visualizing a circadian clock protein: crystal structure of KaiC and functional insights.Semantic proximity Read ↗

Tetrameric architecture of the circadian clock protein KaiB. A novel interface for intermolecular interactions and its impact on the circadian rhythm.Semantic proximity Read ↗

A novel allele of kaiA shortens the circadian period and strengthens interaction of oscillator components in the cyanobacterium Synechococcus elongatus PCC 7942.Semantic proximity Read ↗

Tuning the circadian period of cyanobacteria up to 6.6 days by the single amino acid substitutions in KaiC.Semantic proximity Read ↗

Regulation mechanism study of residues E318/319 for KaiC protein phosphorylation.Semantic proximity Read ↗

Circadian rhythms in the synthesis and degradation of a master clock protein KaiC in cyanobacteria.Semantic proximity Read ↗

Diversity of KaiC-based timing systems in marine Cyanobacteria.Semantic proximity Read ↗

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