PDBsum entry 5h3c

Immune system

PDB id: 5h3c

Contents

Protein chains

158 a.a.

145 a.a.

Waters ×30

PDB id:

5h3c

Name:

Immune system

Title:

Crystal structure of arabidopsis snc1 tir domain

Structure:

Protein suppressor of npr1-1, constitutive 1. Chain: a, b. Fragment: unp residues 17-190. Synonym: atsnc1,disease resistance rpp5-like protein. Engineered: yes

Source:

Arabidopsis thaliana. Mouse-ear cress. Organism_taxid: 3702. Gene: snc1, bal, at4g16890, dl4475c, fcaall.51. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.60Å R-factor: 0.225 R-free: 0.278

Authors:

K.G.Hyun,J.M.Yoon,J.J.Song

Key ref:

K.G.Hyun et al. (2016). Crystal structure of Arabidopsis thaliana SNC1 TIR domain. Biochem Biophys Res Commun, 481, 146-152. PubMed id: 27818198 DOI: 10.1016/j.bbrc.2016.11.004

Date:

22-Oct-16 Release date: 07-Dec-16

Protein chain

O23530  (SNC1_ARATH) -  Protein SUPPRESSOR OF npr1-1, CONSTITUTIVE 1 from Arabidopsis thaliana

Seq: 1437 a.a.

Struc: 158 a.a.

Protein chain

O23530  (SNC1_ARATH) -  Protein SUPPRESSOR OF npr1-1, CONSTITUTIVE 1 from Arabidopsis thaliana

Seq: 1437 a.a.

Struc: 145 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: 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: 10.1016/j.bbrc.2016.11.004

Biochem Biophys Res Commun 481:146-152 (2016)

PubMed id: 27818198

Crystal structure of Arabidopsis thaliana SNC1 TIR domain.

K.G.Hyun, Y.Lee, J.Yoon, H.Yi, J.J.Song.

ABSTRACT

Plant immune response is initiated by Resistance proteins (R proteins). Toll/interleukin-1 receptor (TIR) domain in R proteins, which is responsible for the dimerization but has limited conservation in their primary structures. Suppressor of npr1-1, constitutive 1 (SNC1), a TIR-containing R protein, is involved in autoimmunity of plant, but the binding partner of SNC1 via the TIR domain and its specific cognate effector protein remain elusive. Here, we present the crystal structure of the TIR domain of Arabidopsis thaliana SNC1 (AtSNC1-TIR). The structure shows that AtSNC1-TIR domain is similar to those of other plant TIR domains including AtTIR, L6 and RPS4. Structural and sequence analysis on AtSNC1-TIR revealed that almost all conserved amino acids are located in the core of the structure, while the amino acids on the surface are highly variable, implicating that each TIR domain utilizes the variable surface for interacting its binding partner. In addition, the interaction between AtSNC1-TIR proteins in the crystal suggests two possible dimerization modes of AtSNC1-TIR domain. This study provides structural platform to investigate AtSNC1-TIR mediated signaling pathway of plant immune responses.