4I92

Structure of the BSK8 kinase domain

4I92 の概要

• エントリーDOI: 10.2210/pdb4i92/pdb
• 関連するPDBエントリー: 4I93 4I94
• 分子名称: Probable serine/threonine-protein kinase At5g41260, CHLORIDE ION (3 entities in total)
• 機能のキーワード: protein kinase, pseudo kinase, cfg, alanine gatekeeper, transferase brassinosteroid-signaling, transferase
• 由来する生物種: Arabidopsis thaliana (mouse-ear cress,thale-cress)
• 細胞内の位置: Cell membrane; Lipid-anchor (Potential): Q9FHD7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34423.64

構造登録者

Gruetter, C.,Rauh, D. (登録日: 2012-12-04, 公開日: 2013-08-14, 最終更新日: 2024-03-20)

主引用文献

Grutter, C.,Sreeramulu, S.,Sessa, G.,Rauh, D.
Structural Characterization of the RLCK Family Member BSK8: A Pseudokinase with an Unprecedented Architecture
J.Mol.Biol., 425:4455-4467, 2013

PubMed Abstract: Brassinosteroid signaling kinases (BSKs) are plant-specific receptor-like cytoplasmic protein kinases involved in the brassinosteroid signaling pathway. Unlike common protein kinases, they possess a naturally occurring alanine residue at the "gatekeeper" position, as well as other sequence variations. How BSKs activate downstream proteins such as BSU1, as well as the structural consequences of their unusual sequential features, was unclear. We crystallized the catalytic domain of BSK8 and solved its structure by multiple-wavelength anomalous dispersion phasing methods to a resolution of 1.5Å. In addition, a co-crystal structure of BSK8 with 5-adenylyl imidodiphosphate (AMP-PNP) revealed unusual conformational arrangements of the nucleotide phosphate groups and catalytic key motifs, typically not observed for active protein kinases. Sequential analysis and comparisons with known pseudokinase structures suggest that BSKs represent constitutively inactive protein kinases that regulate brassinosteroid signal transfer through an allosteric mechanism.

PubMed: 23911552
DOI: 10.1016/j.jmb.2013.07.034

実験手法

X-RAY DIFFRACTION (1.6 Å)