3PPZ

Crystal structure of CTR1 kinase domain in complex with staurosporine

3PPZ の概要

• エントリーDOI: 10.2210/pdb3ppz/pdb
• 関連するPDBエントリー: 3P86
• 分子名称: Serine/threonine-protein kinase CTR1, STAUROSPORINE (2 entities in total)
• 機能のキーワード: kinase, atp binding, phosphorylation, transferase
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71385.31

構造登録者

Mayerhofer, H.,Panneerselvam, S.,Mueller-Dieckmann, J. (登録日: 2010-11-25, 公開日: 2011-12-07, 最終更新日: 2024-11-13)

主引用文献

Mayerhofer, H.,Panneerselvam, S.,Mueller-Dieckmann, J.
Protein kinase domain of CTR1 from Arabidopsis thaliana promotes ethylene receptor cross talk.
J. Mol. Biol., 415:768-779, 2012

PubMed Abstract: Ethylene controls many aspects of plant growth and development. Signaling by the gaseous phytohormone is initiated by disulfide-linked membrane-bound receptors, and the formation of heteromeric receptor clusters contributes to the broad range of ethylene responsiveness. In Arabidopsis thaliana, the TCS-like ethylene receptors interact with the cytosolic serine/threonine kinase constitutive triple response 1 (CTR1), a proposed mitogen-activated protein kinase kinase kinase. In the absence of the hormone, the receptor and therefore CTR1 are active. Hence, ethylene acts as an inverse agonist of its signaling pathway. The three-dimensional structures of the active, triphosphorylated and the unphosphorylated, inactive kinase domain of CTR1 in complex with staurosporine illustrate the conformational rearrangements that form the basis of activity regulation. Additionally, in analytical ultracentrifugation experiments, active kinase domains form back-to-back dimers, while inactive and activation loop variants are monomers. Together with a front-to-front activation interface, the active protein kinase dimers thereby engage in interactions that promote CTR1-mediated cross talk between ethylene receptor clusters. This model provides a structural foundation for the observed high sensitivity of plants to ethylene.

PubMed: 22155294
DOI: 10.1016/j.jmb.2011.11.046

実験手法

X-RAY DIFFRACTION (2.99 Å)