1V2Z

Crystal structure of the C-terminal domain of Thermosynechococcus elongatus BP-1 KaiA

1V2Z の概要

• エントリーDOI: 10.2210/pdb1v2z/pdb
• 分子名称: circadian clock protein KaiA homolog (2 entities in total)
• 機能のキーワード: all alpha, riken structural genomics/proteomics initiative, rsgi, structural genomics, circadian clock protein
• 由来する生物種: Thermosynechococcus elongatus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13186.21

構造登録者

Uzumaki, T.,Fujita, M.,Nakatsu, T.,Hayashi, F.,Shibata, H.,Itoh, N.,Kato, H.,Ishiura, M.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2003-10-20, 公開日: 2004-06-01, 最終更新日: 2023-12-27)

主引用文献

Uzumaki, T.,Fujita, M.,Nakatsu, T.,Hayashi, F.,Shibata, H.,Itoh, N.,Kato, H.,Ishiura, M.
Crystal structure of the C-terminal clock-oscillator domain of the cyanobacterial KaiA protein
NAT.STRUCT.MOL.BIOL., 11:623-631, 2004

PubMed Abstract: KaiA, KaiB and KaiC constitute the circadian clock machinery in cyanobacteria, and KaiA activates kaiBC expression whereas KaiC represses it. Here we show that KaiA is composed of three functional domains, the N-terminal amplitude-amplifier domain, the central period-adjuster domain and the C-terminal clock-oscillator domain. The C-terminal domain is responsible for dimer formation, binding to KaiC, enhancing KaiC phosphorylation and generating the circadian oscillations. The X-ray crystal structure at a resolution of 1.8 A of the C-terminal clock-oscillator domain of KaiA from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1 shows that residue His270, located at the center of a KaiA dimer concavity, is essential to KaiA function. KaiA binding to KaiC probably occurs via the concave surface. On the basis of the structure, we predict the structural roles of the residues that affect circadian oscillations.

PubMed: 15170179
DOI: 10.1038/nsmb781

実験手法

X-RAY DIFFRACTION (1.8 Å)