3K0C

Crystal structure of the phosphorylation-site double mutant S431A/T432E of the KaiC circadian clock protein

3K0C の概要

• エントリーDOI: 10.2210/pdb3k0c/pdb
• 関連するPDBエントリー: 3DVL 3JZM 3K09 3K0A 3K0E 3K0F
• 分子名称: Circadian clock protein kinase KaiC, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: kaic, circadian clock protein, kinase, hexamer, atp-binding, biological rhythms, dna-binding, magnesium, metal-binding, nucleotide-binding, phosphoprotein, repressor, serine/threonine-protein kinase, transcription, transcription regulation, transferase
• 由来する生物種: Synechococcus elongatus PCC 7942 (Anacystis nidulans R2); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 355449.51

構造登録者

Pattanayek, R.,Egli, M.,Pattanayek, S. (登録日: 2009-09-24, 公開日: 2010-03-31, 最終更新日: 2024-11-27)

主引用文献

Pattanayek, R.,Mori, T.,Xu, Y.,Pattanayek, S.,Johnson, C.H.,Egli, M.
Structures of KaiC Circadian Clock Mutant Proteins: A New Phosphorylation Site at T426 and Mechanisms of Kinase, ATPase and Phosphatase.
Plos One, 4:e7529-e7529, 2009

PubMed Abstract: 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 order (TS-->pTS-->pTpS-->TpS-->TS) over the daily cycle, the origin of which is not understood. To address this void and to analyze the roles of KaiC active site residues, in particular T426, we determined structures of single and double P-site mutants of S. elongatus KaiC.

PubMed: 19956664
DOI: 10.1371/journal.pone.0007529

実験手法

X-RAY DIFFRACTION (3.3 Å)