3SV0

Crystal structure of casein kinase-1 like protein in plant

3SV0 の概要

• エントリーDOI: 10.2210/pdb3sv0/pdb
• 分子名称: Casein kinase I-like (2 entities in total)
• 機能のキーワード: kinase, typical kinase domain fold, cytosol, transferase
• 由来する生物種: Oryza sativa Japonica Group (Japanese rice)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54270.16

構造登録者

Park, H.H.,Do, K.H. (登録日: 2011-07-12, 公開日: 2012-06-20, 最終更新日: 2024-03-20)

主引用文献

Park, Y.I.,Do, K.H.,Kim, I.S.,Park, H.H.
Structural and functional studies of casein kinase I-like protein from rice
Plant Cell.Physiol., 53:304-311, 2012

PubMed Abstract: Casein kinase I (CKI) is a protein serine/threonine kinase that is highly conserved from plants to animals. It performs various functions in both the cytoplasm and nucleus, such as DNA repair, cell cycle, cytokinesis, vesicular trafficking, morphogenesis and circadian rhythm. CKI proteins contain a highly conserved kinase domain responsible for catalytic activity at the N-terminus and a highly diverse regulatory domain responsible for determining substrate specificity at the C-terminus. CKI-like protein has been identified in plants, including in rice, but its function and structure have not been reported. Here, we report the 2.0 Å crystal structure of the kinase domain of CKI-like protein from rice. Although the structure adopts the typical bi-lobal kinase architecture, the length and orientation of the glycine-rich ATP-binding motif are dynamic within the CKI family. A loop between α5 and α6 (the α5-α6 loop), which was previously not detected in the CKI family because of flexibility, was clearly detected in our structure. In addition, we identified a lipase as a substrate of CKI-like protein from rice. Phosphorylation of the lipase dramatically reduced its catalytic activity, suggesting that CKI may play a role in the regulation of lipase activity.

PubMed: 22199373
DOI: 10.1093/pcp/pcr175

実験手法

X-RAY DIFFRACTION (2 Å)