5H3C

Crystal structure of Arabidopsis SNC1 TIR domain

5H3C の概要

• エントリーDOI: 10.2210/pdb5h3c/pdb
• 分子名称: Protein SUPPRESSOR OF npr1-1, CONSTITUTIVE 1 (2 entities in total)
• 機能のキーワード: plant, immunity, rprotein, immune system
• 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: 40068.32

構造登録者

Hyun, K.G.,Yoon, J.M.,Song, J.J. (登録日: 2016-10-22, 公開日: 2016-12-07, 最終更新日: 2024-10-23)

主引用文献

Hyun, K.G.,Lee, Y.,Yoon, J.,Yi, H.,Song, J.J.
Crystal structure of Arabidopsis thaliana SNC1 TIR domain
Biochem.Biophys.Res.Commun., 481:146-152, 2016

PubMed Abstract: Plant immune response is initiated by Resistance proteins (R proteins). Toll/interleukin-1 receptor (TIR) domain in R proteins, which is responsible for the dimerization but has limited conservation in their primary structures. Suppressor of npr1-1, constitutive 1 (SNC1), a TIR-containing R protein, is involved in autoimmunity of plant, but the binding partner of SNC1 via the TIR domain and its specific cognate effector protein remain elusive. Here, we present the crystal structure of the TIR domain of Arabidopsis thaliana SNC1 (AtSNC1-TIR). The structure shows that AtSNC1-TIR domain is similar to those of other plant TIR domains including AtTIR, L6 and RPS4. Structural and sequence analysis on AtSNC1-TIR revealed that almost all conserved amino acids are located in the core of the structure, while the amino acids on the surface are highly variable, implicating that each TIR domain utilizes the variable surface for interacting its binding partner. In addition, the interaction between AtSNC1-TIR proteins in the crystal suggests two possible dimerization modes of AtSNC1-TIR domain. This study provides structural platform to investigate AtSNC1-TIR mediated signaling pathway of plant immune responses.

PubMed: 27818198
DOI: 10.1016/j.bbrc.2016.11.004

実験手法

X-RAY DIFFRACTION (2.596 Å)