3ZUT

The structure of OST1 (D160A) kinase

3ZUT の概要

• エントリーDOI: 10.2210/pdb3zut/pdb
• 関連するPDBエントリー: 3ZUU
• 分子名称: Serine/threonine-protein kinase SRK2E (2 entities in total)
• 機能のキーワード: transferase, kinase regulation, plant abiotic stress, signaling
• 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: 82104.98

構造登録者

Yunta, C.,Martinez-Ripoll, M.,Albert, A. (登録日: 2011-07-20, 公開日: 2011-10-12, 最終更新日: 2023-12-20)

主引用文献

Yunta, C.,Martinez-Ripoll, M.,Zhu, J.K.,Albert, A.
The structure of Arabidopsis thaliana OST1 provides insights into the kinase regulation mechanism in response to osmotic stress.
J. Mol. Biol., 414:135-144, 2011

PubMed Abstract: SnRK [SNF1 (sucrose non-fermenting-1)-related protein kinase] 2.6 [open stomata 1 (OST1)] is well characterized at molecular and physiological levels to control stomata closure in response to water-deficit stress. OST1 is a member of a family of 10 protein kinases from Arabidopsis thaliana (SnRK2) that integrates abscisic acid (ABA)-dependent and ABA-independent signals to coordinate the cell response to osmotic stress. A subgroup of protein phosphatases type 2C binds OST1 and keeps the kinase dephosphorylated and inactive. Activation of OST1 relies on the ABA-dependent inhibition of the protein phosphatases type 2C and the subsequent self-phosphorylation of the kinase. The OST1 ABA-independent activation depends on a short sequence motif that is conserved among all the members of the SnRK2 family. However, little is known about the molecular mechanism underlying this regulation. The crystallographic structure of OST1 shows that ABA-independent regulation motif stabilizes the conformation of the kinase catalytically essential α C helix, and it provides the basis of the ABA-independent regulation mechanism for the SnRK2 family of protein kinases.

PubMed: 21983340
DOI: 10.1016/j.jmb.2011.09.041

実験手法

X-RAY DIFFRACTION (2.5 Å)