5TEC
Crystal structure of the TIR domain from the Arabidopsis thaliana NLR protein SNC1
5TEC の概要
| エントリーDOI | 10.2210/pdb5tec/pdb |
| 関連するPDBエントリー | 5TEB |
| 分子名称 | Protein SUPPRESSOR OF npr1-1, CONSTITUTIVE 1 (2 entities in total) |
| 機能のキーワード | tir domain, plant nlr, 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 | 39693.16 |
| 構造登録者 | Zhang, X.,Bentham, A.,Ve, T.,Williams, S.J.,Kobe, B. (登録日: 2016-09-20, 公開日: 2017-02-01, 最終更新日: 2023-10-04) |
| 主引用文献 | Zhang, X.,Bernoux, M.,Bentham, A.R.,Newman, T.E.,Ve, T.,Casey, L.W.,Raaymakers, T.M.,Hu, J.,Croll, T.I.,Schreiber, K.J.,Staskawicz, B.J.,Anderson, P.A.,Sohn, K.H.,Williams, S.J.,Dodds, P.N.,Kobe, B. Multiple functional self-association interfaces in plant TIR domains. Proc. Natl. Acad. Sci. U.S.A., 114:E2046-E2052, 2017 Cited by PubMed Abstract: The self-association of Toll/interleukin-1 receptor/resistance protein (TIR) domains has been implicated in signaling in plant and animal immunity receptors. Structure-based studies identified different TIR-domain dimerization interfaces required for signaling of the plant nucleotide-binding oligomerization domain-like receptors (NLRs) L6 from flax and disease resistance protein RPS4 from Here we show that the crystal structure of the TIR domain from the NLR suppressor of npr1-1, constitutive 1 (SNC1) contains both an L6-like interface involving helices αD and αE (DE interface) and an RPS4-like interface involving helices αA and αE (AE interface). Mutations in either the AE- or DE-interface region disrupt cell-death signaling activity of SNC1, L6, and RPS4 TIR domains and full-length L6 and RPS4. Self-association of L6 and RPS4 TIR domains is affected by mutations in either region, whereas only AE-interface mutations affect SNC1 TIR-domain self-association. We further show two similar interfaces in the crystal structure of the TIR domain from the NLR recognition of 1 (RPP1). These data demonstrate that both the AE and DE self-association interfaces are simultaneously required for self-association and cell-death signaling in diverse plant NLRs. PubMed: 28159890DOI: 10.1073/pnas.1621248114 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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