PDBsum entry 5teb

Signaling protein

PDB id: 5teb

Contents

Protein chains

(+ 2 more) 166 a.a.

PDB id:

5teb

Name:

Signaling protein

Title:

Crystal structure of the tir domain from the arabidopsis thaliana disease resistance protein rpp1

Structure:

Recognition of peronospora parasitica 1. Chain: a, b, c, d, e, f, g, h. Engineered: yes

Source:

Arabidopsis thaliana. Mouse-ear cress. Organism_taxid: 3702. Gene: rpp1. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.80Å R-factor: 0.220 R-free: 0.269

Authors:

A.R.Bentham,X.Zhang,T.Croll,S.Williams,B.Kobe

Key ref:

X.Zhang et al. (2017). Multiple functional self-association interfaces in plant TIR domains. Proc Natl Acad Sci U S A, 114, E2046. PubMed id: 28159890 DOI: 10.1073/pnas.1621248114

Date:

20-Sep-16 Release date: 01-Feb-17

Protein chains

D9IW02  (D9IW02_ARATH) -  ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase from Arabidopsis thaliana

Seq: 1154 a.a.

Struc: 166 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.2.2.6 - ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase.
• Reaction: NAD⁺ + H2O = ADP-D-ribose + nicotinamide + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1073/pnas.1621248114

Proc Natl Acad Sci U S A 114:E2046 (2017)

PubMed id: 28159890

Multiple functional self-association interfaces in plant TIR domains.

X.Zhang, M.Bernoux, A.R.Bentham, T.E.Newman, T.Ve, L.W.Casey, T.M.Raaymakers, J.Hu, T.I.Croll, K.J.Schreiber, B.J.Staskawicz, P.A.Anderson, K.H.Sohn, S.J.Williams, P.N.Dodds, B.Kobe.

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 Arabidopsis Here we show that the crystal structure of the TIR domain from the Arabidopsis 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 Arabidopsis NLR recognition of Peronospora parasitica 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.