4C6R

Crystal structure of the TIR domain from the Arabidopsis Thaliana disease resistance protein RPS4

4C6R の概要

• エントリーDOI: 10.2210/pdb4c6r/pdb
• 関連するPDBエントリー: 4C6S 4C6T
• 分子名称: DISEASE RESISTANCE PROTEIN RPS4 (2 entities in total)
• 機能のキーワード: immune system, plant tir domain, signal transduction
• 由来する生物種: ARABIDOPSIS THALIANA
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 78454.99

構造登録者

Williams, S.J.,Sohn, K.H.,Wan, L.,Bernoux, M.,Ma, Y.,Segonzac, C.,Ve, T.,Sarris, P.,Ericsson, D.J.,Saucet, S.B.,Zhang, X.,Parker, J.,Dodds, P.N.,Jones, J.D.G.,Kobe, B. (登録日: 2013-09-19, 公開日: 2014-05-28, 最終更新日: 2023-12-20)

主引用文献

Williams, S.J.,Sohn, K.H.,Wan, L.,Bernoux, M.,Sarris, P.F.,Segonzac, C.,Ve, T.,Ma, Y.,Saucet, S.B.,Ericsson, D.J.,Casey, L.W.,Lonhienne, T.,Winzor, D.J.,Zhang, X.,Coerdt, A.,Parker, J.E.,Dodds, P.N.,Kobe, B.,Jones, J.D.G.
Structural Basis for Assembly and Function of a Heterodimeric Plant Immune Receptor.
Science, 344:299-, 2014

PubMed Abstract: Cytoplasmic plant immune receptors recognize specific pathogen effector proteins and initiate effector-triggered immunity. In Arabidopsis, the immune receptors RPS4 and RRS1 are both required to activate defense to three different pathogens. We show that RPS4 and RRS1 physically associate. Crystal structures of the N-terminal Toll-interleukin-1 receptor/resistance (TIR) domains of RPS4 and RRS1, individually and as a heterodimeric complex (respectively at 2.05, 1.75, and 2.65 angstrom resolution), reveal a conserved TIR/TIR interaction interface. We show that TIR domain heterodimerization is required to form a functional RRS1/RPS4 effector recognition complex. The RPS4 TIR domain activates effector-independent defense, which is inhibited by the RRS1 TIR domain through the heterodimerization interface. Thus, RPS4 and RRS1 function as a receptor complex in which the two components play distinct roles in recognition and signaling.

PubMed: 24744375
DOI: 10.1126/SCIENCE.1247357

実験手法

X-RAY DIFFRACTION (2.05 Å)