6LKB

Crystal Structure of the peptidylprolyl isomerase domain of Arabidopsis thaliana CYP71.

6LKB の概要

• エントリーDOI: 10.2210/pdb6lkb/pdb
• 分子名称: Peptidyl-prolyl cis-trans isomerase CYP71, GLYCEROL, COBALT (II) ION, ... (6 entities in total)
• 機能のキーワード: ppiase, cyp71, cyclophilin, chromatin remodelling, isomerase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36853.76

構造登録者

Lakhanpal, S.,Jobichen, C.,Swaminathan, K. (登録日: 2019-12-18, 公開日: 2020-12-16, 最終更新日: 2023-11-22)

主引用文献

Lakhanpal, S.,Fan, J.S.,Luan, S.,Swaminathan, K.
Structural and functional analyses of the PPIase domain of Arabidopsis thaliana CYP71 reveal its catalytic activity toward histone H3.
Febs Lett., 595:145-154, 2021

PubMed Abstract: Arabidopsis thaliana CYP71 (AtCYP71) is a chromatin-remodeling protein that promotes shoot apical meristem (SAM) differentiation. The N terminus of AtCYP71 contains a noncanonical WD domain, and the C terminus contains an enzymatic peptidyl-prolyl isomerase (PPIase) cyclophilin (CYP) domain. To date, there has been no characterization of CYP71, and its mode of action remains unknown. Here, we report the crystal structure of the CYP domain of AtCYP71 at 1.9 Å resolution. The structure shows key differences when compared to the canonical CYP fold of human CypA. To the best our knowledge, this is the first A. thaliana CYP structure with a conserved active site loop. Using nuclear magnetic resonance spectroscopy, we demonstrate that the CYP domain is active toward histone H3. Our findings suggest that the PPIase activity of the CYP domain is important for the function of AtCYP71 in chromatin remodeling during organogenesis.

PubMed: 33098102
DOI: 10.1002/1873-3468.13965

実験手法

X-RAY DIFFRACTION (1.651 Å)