PDBsum entry 4c6t

Immune system

PDB id: 4c6t

Contents

Protein chains

141 a.a.

166 a.a.

Ligands

MLA ×2

PDB id:

4c6t

Name:

Immune system

Title:

Crystal structure of the rps4 and rrs1 tir domain heterodimer

Structure:

Probable wrky transcription factor 52. Chain: a, c. Fragment: toll/interleukin-1 receptor domain, residues 6-153. Synonym: disease resistance protein rrs1, disease resistance protein slh1, protein sensitive to low humidity 1, resistance to ralstoni a solanacearum 1 protein, wrky DNA-binding protein 52. Engineered: yes. Disease resistance protein rps4. Chain: b, d.

Source:

Arabidopsis thaliana. Organism_taxid: 3702. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta.

Resolution:

2.65Å R-factor: 0.185 R-free: 0.227

Authors:

S.J.Williams,K.H.Sohn,L.Wan,M.Bernoux,Y.Ma,C.Segonzac,T.Ve,P.Sarris, D.J.Ericsson,S.B.Saucet,X.Zhang,J.Parker,P.N.Dodds,J.D.G.Jones, B.Kobe

Key ref:

S.J.Williams et al. (2014). Structural basis for assembly and function of a heterodimeric plant immune receptor. Science, 344, 299-303. PubMed id: 24744375 DOI: 10.1126/science.1247357

Date:

19-Sep-13 Release date: 28-May-14

Protein chains

P0DKH5  (WR52C_ARATH) -  Disease resistance protein RRS1 from Arabidopsis thaliana

Seq: 1288 a.a.

Struc: 141 a.a.

Protein chains

Q9XGM3  (RPS4C_ARATH) -  Disease resistance protein RPS4 from Arabidopsis thaliana

Seq: 1217 a.a.

Struc: 166 a.a.

Enzyme reactions

• Enzyme class: Chains B, D: 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: 10.1126/science.1247357

Science 344:299-303 (2014)

PubMed id: 24744375

Structural basis for assembly and function of a heterodimeric plant immune receptor.

S.J.Williams, K.H.Sohn, L.Wan, M.Bernoux, P.F.Sarris, C.Segonzac, T.Ve, Y.Ma, S.B.Saucet, D.J.Ericsson, L.W.Casey, T.Lonhienne, D.J.Winzor, X.Zhang, A.Coerdt, J.E.Parker, P.N.Dodds, B.Kobe, J.D.Jones.

ABSTRACT

Cytoplasmic plant immune receptors recognize specific pathogen effector proteins and initiate effector-triggered immunity. In Arabidopsis, the immune receptors RPS4 and RRS1 are both required to activate defense to three different pathogens. We show that RPS4 and RRS1 physically associate. Crystal structures of the N-terminal Toll-interleukin-1 receptor/resistance (TIR) domains of RPS4 and RRS1, individually and as a heterodimeric complex (respectively at 2.05, 1.75, and 2.65 angstrom resolution), reveal a conserved TIR/TIR interaction interface. We show that TIR domain heterodimerization is required to form a functional RRS1/RPS4 effector recognition complex. The RPS4 TIR domain activates effector-independent defense, which is inhibited by the RRS1 TIR domain through the heterodimerization interface. Thus, RPS4 and RRS1 function as a receptor complex in which the two components play distinct roles in recognition and signaling.