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Article

Visualizing a circadian clock protein: crystal structure of KaiC and functional insights.

Molecular cell - 13 Aug 2004

Pattanayek Rekha, Wang Jimin, Mori Tetsuya, Xu Yao, Johnson Carl Hirschie, Egli Martin

Abstract excerpt

Circadian (daily) biological clocks express characteristics that are difficult to explain by known biochemical mechanisms, and will ultimately require characterizing the structures, functions, and interactions of their molecular components. KaiC is an essential circadian protein in cyanobacteria that forms the core of the KaiABC clock protein complex. We report the crystal structure of the KaiC homohexameric...

Topics

Adenosine Triphosphate
Bacterial Proteins
Circadian Rhythm
Circadian Rhythm Signaling Peptides and Proteins
Cyanobacteria
Evolution, Molecular
Lighting
Mutation
Phosphorylation
Protein Structure, Tertiary

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 15304218
DOI: 10.1016/j.molcel.2004.07.013

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-15304218-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Visualizing a circadian clock protein: crystal structure of KaiC and functional insights.PMID 15304218Read ↗

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

Anabaena circadian clock proteins KaiA and KaiB reveal a potential common binding site to their partner KaiC.Semantic proximity Read ↗

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

The roles of the dimeric and tetrameric structures of the clock protein KaiB in the generation of circadian oscillations in cyanobacteria.Semantic proximity Read ↗

Structural characterization of the circadian clock protein complex composed of KaiB and KaiC by inverse contrast-matching small-angle neutron scattering.Semantic proximity Read ↗

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

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

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

Two KaiA-binding domains of cyanobacterial circadian clock protein KaiC.Semantic proximity Read ↗

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