3OZI

Crystal structure of the TIR domain from the flax disease resistance protein L6

3OZI の概要

• エントリーDOI: 10.2210/pdb3ozi/pdb
• 分子名称: L6tr, COBALT (II) ION (3 entities in total)
• 機能のキーワード: plant tir domain, signal transduction, plant protein
• 由来する生物種: Linum usitatissimum (Flax)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46913.31

構造登録者

Ve, T.,Bernoux, M.,Williams, S.,Valkov, E.,Warren, C.,Hatters, D.,Ellis, J.G.,Dodds, P.N.,Kobe, B. (登録日: 2010-09-25, 公開日: 2011-04-27, 最終更新日: 2023-11-01)

主引用文献

Bernoux, M.,Ve, T.,Williams, S.,Warren, C.,Hatters, D.,Valkov, E.,Zhang, X.,Ellis, J.G.,Kobe, B.,Dodds, P.N.
Structural and Functional Analysis of a Plant Resistance Protein TIR Domain Reveals Interfaces for Self-Association, Signaling, and Autoregulation.
Cell Host Microbe, 9:200-211, 2011

PubMed Abstract: The Toll/interleukin-1 receptor (TIR) domain occurs in animal and plant immune receptors. In the animal Toll-like receptors, homodimerization of the intracellular TIR domain is required for initiation of signaling cascades leading to innate immunity. By contrast, the role of the TIR domain in cytoplasmic nucleotide-binding/leucine-rich repeat (NB-LRR) plant immune resistance proteins is poorly understood. L6 is a TIR-NB-LRR resistance protein from flax (Linum usitatissimum) that confers resistance to the flax rust phytopathogenic fungus (Melampsora lini). We determine the crystal structure of the L6 TIR domain and show that, although dispensable for pathogenic effector protein recognition, the TIR domain alone is both necessary and sufficient for L6 immune signaling. We demonstrate that the L6 TIR domain self-associates, most likely forming a homodimer. Analysis of the structure combined with site-directed mutagenesis suggests that self-association is a requirement for immune signaling and reveals distinct surface regions involved in self-association, signaling, and autoregulation.

PubMed: 21402359
DOI: 10.1016/j.chom.2011.02.009

実験手法

X-RAY DIFFRACTION (2.3 Å)