5TEC

Crystal structure of the TIR domain from the Arabidopsis thaliana NLR protein SNC1

Summary for 5TEC

• Entry DOI: 10.2210/pdb5tec/pdb
• Related: 5TEB
• Descriptor: Protein SUPPRESSOR OF npr1-1, CONSTITUTIVE 1 (2 entities in total)
• Functional Keywords: tir domain, plant nlr, immune system
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 2
• Total formula weight: 39693.16

Authors

Zhang, X.,Bentham, A.,Ve, T.,Williams, S.J.,Kobe, B. (deposition date: 2016-09-20, release date: 2017-02-01, Last modification date: 2023-10-04)

Primary citation

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

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: 28159890
DOI: 10.1073/pnas.1621248114

Experimental method

X-RAY DIFFRACTION (2.2 Å)