5JYK

Deg9 crystal under 289K

5JYK の概要

• エントリーDOI: 10.2210/pdb5jyk/pdb
• 分子名称: Protease Do-like 9, GLYCEROL (3 entities in total)
• 機能のキーワード: deg protease, hydrolase
• 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: 124856.86

構造登録者

Ouyang, M.,Zhang, L.X. (登録日: 2016-05-14, 公開日: 2017-05-31, 最終更新日: 2023-11-08)

主引用文献

Ouyang, M.,Li, X.,Zhao, S.,Pu, H.,Shen, J.,Adam, Z.,Clausen, T.,Zhang, L.
The crystal structure of Deg9 reveals a novel octameric-type HtrA protease
Nat Plants, 3:973-982, 2017

PubMed Abstract: The high temperature requirement A (HtrA) proteases (also termed Deg proteases) play important roles in diverse organisms by regulating protein quality and quantity. One of the 16 Arabidopsis homologs, Deg9, is located in the nucleus where it modulates cytokinin- and light-mediated signalling via degrading the ARABIDOPSIS RESPONSE REGULATOR 4 (ARR4). To uncover the structural features underlying the proteolytic activity of Deg9, we determined its crystal structure. Unlike the well-established trimeric building block of HtrAs, Deg9 displays a novel octameric structure consisting of two tetrameric rings that have distinct conformations. Based on the structural architecture, we generated several mutant variants of Deg9, determined their structure and tested their proteolytic activity towards ARR4. The results of the structural and biochemical analyses allowed us to propose a model for a novel mechanism of substrate recognition and activity regulation of Deg9. In this model, protease activation of one tetramer is mediated by en-bloc reorientation of the protease domains to open an entrance for the substrate in the opposite (inactive) tetramer. This study provides the structural basis for understanding how the levels of nuclear signal components are regulated by a plant protease.

PubMed: 29180814
DOI: 10.1038/s41477-017-0060-2

実験手法

X-RAY DIFFRACTION (2.297 Å)