1Q6B

Solution Structure of the C-terminal Domain of Thermosynechococcus elongatus KaiA (ThKaiA180C); Ensemble of 25 Structures

1Q6B の概要

• エントリーDOI: 10.2210/pdb1q6b/pdb
• 関連するPDBエントリー: 1Q6A
• NMR情報: BMRB: 5824
• 分子名称: Circadian clock protein KaiA homolog (1 entity in total)
• 機能のキーワード: all alpha-helix protein, homodimer, circadian clock protein
• 由来する生物種: Thermosynechococcus elongatus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25203.17

構造登録者

Vakonakis, I.,Sun, J.,Golden, S.S.,Holzenburg, A.,LiWang, A.C. (登録日: 2003-08-13, 公開日: 2003-08-19, 最終更新日: 2024-11-20)

主引用文献

Vakonakis, I.,Sun, J.,Wu, T.,Holzenburg, A.,Golden, S.S.,LiWang, A.C.
NMR structure of the KaiC-interacting C-terminal domain of KaiA, a circadian clock protein: implications for KaiA-KaiC interaction
Proc.Natl.Acad.Sci.USA, 101:1479-1484, 2004

PubMed Abstract: KaiA is a two-domain circadian clock protein in cyanobacteria, acting as the positive element in a feedback loop that sustains the oscillation. The structure of the N-terminal domain of KaiA is that of a pseudo-receiver, similar to those of bacterial response regulators, which likely interacts with components of the clock-resetting pathway. The C-terminal domain of KaiA is highly conserved among cyanobacteria and enhances the autokinase activity of KaiC. Here we present the NMR structure of the C-terminal domain of KaiA from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1. This domain adopts a novel all alpha-helical homodimeric structure. Several mutations known to affect the period of the circadian oscillator are shown to be located at an exposed groove near the dimer interface. This NMR structure and a 21-A-resolution electron microscopy structure of the hexameric KaiC particle allow us to postulate a mode of KaiA-KaiC interaction, in which KaiA binds a linker region connecting two globular KaiC domains.

PubMed: 14749515
DOI: 10.1073/pnas.0305516101

実験手法

SOLUTION NMR