3JRN
Crystal structure of TIR domain from Arabidopsis Thaliana
3JRN の概要
エントリーDOI | 10.2210/pdb3jrn/pdb |
分子名称 | AT1G72930 protein, ARSENIC (3 entities in total) |
機能のキーワード | tir domain arabidopsis thaliana, plant protein |
由来する生物種 | Arabidopsis thaliana (mouse-ear cress,thale-cress) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 20349.88 |
構造登録者 | Chan, S.L.,Mukasa, T.,Santelli, E.,Low, L.Y.,Pascual, J. (登録日: 2009-09-08, 公開日: 2009-10-20, 最終更新日: 2024-02-21) |
主引用文献 | Chan, S.L.,Mukasa, T.,Santelli, E.,Low, L.Y.,Pascual, J. The crystal structure of a TIR domain from Arabidopsis thaliana reveals a conserved helical region unique to plants. Protein Sci., 19:155-161, 2009 Cited by PubMed Abstract: Plants use a highly evolved immune system to exhibit defense response against microbial infections. The plant TIR domain, together with the nucleotide-binding (NB) domain and/or a LRR region, forms a type of molecule, named resistance (R) proteins, that interact with microbial effector proteins and elicit hypersensitive responses against infection. Here, we report the first crystal structure of a plant TIR domain from Arabidopsis thaliana (AtTIR) solved at a resolution of 2.0 A. The structure consists of five beta-strands forming a parallel beta-sheet at the core of the protein. The beta-strands are connected by a series of alpha-helices and the overall fold mimics closely that of other mammalian and bacterial TIR domains. However, the region of the alphaD-helix reveals significant differences when compared with other TIR structures, especially the alphaD3-helix that corresponds to an insertion only present in plant TIR domains. Available mutagenesis data suggest that several conserved and exposed residues in this region are involved in the plant TIR signaling function. PubMed: 19845004DOI: 10.1002/pro.275 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
構造検証レポート
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