6XX8

Arabidopsis thaliana Casein Kinase 2 (CK2) alpha-1 crystal form II

6XX8 の概要

• エントリーDOI: 10.2210/pdb6xx8/pdb
• 分子名称: Casein kinase II subunit alpha-1 (2 entities in total)
• 機能のキーワード: kinase, ck2, casein kinase, cell cycle
• 由来する生物種: Arabidopsis thaliana (thale cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81043.02

構造登録者

Demulder, M.,De Veylder, L.,Loris, R. (登録日: 2020-01-27, 公開日: 2020-04-15, 最終更新日: 2024-01-24)

主引用文献

Demulder, M.,De Veylder, L.,Loris, R.
Crystal structure of Arabidopsis thaliana casein kinase 2 alpha 1.
Acta Crystallogr.,Sect.F, 76:182-191, 2020

PubMed Abstract: Casein kinase 2 (CK2) is a ubiquitous pleiotropic enzyme that is highly conserved across eukaryotic kingdoms. CK2 is singular amongst kinases as it is highly rigid and constitutively active. Arabidopsis thaliana is widely used as a model system in molecular plant research; the biological functions of A. thaliana CK2 are well studied in vivo and many of its substrates have been identified. Here, crystal structures of the α subunit of A. thaliana CK2 in three crystal forms and of its complex with the nonhydrolyzable ATP analog AMppNHp are presented. While the C-lobe of the enzyme is highly rigid, structural plasticity is observed for the N-lobe. Small but significant displacements within the active cleft are necessary in order to avoid steric clashes with the AMppNHp molecule. Binding of AMppNHp is influenced by a rigid-body motion of the N-lobe that was not previously recognized in maize CK2.

PubMed: 32254052
DOI: 10.1107/S2053230X20004537

実験手法

X-RAY DIFFRACTION (1.8 Å)