5KU7

Crystal structure of the TIR domain from the Muscadinia rotundifolia disease resistance protein RPV1

Summary for 5KU7

• Entry DOI: 10.2210/pdb5ku7/pdb
• Descriptor: TIR-NB-LRR type resistance protein RPV1, MALONIC ACID (3 entities in total)
• Functional Keywords: tir domain, plant nlr, signaling protein
• Biological source: Vitis rotundifolia (Muscadine grape)
• Total number of polymer chains: 2
• Total formula weight: 41694.68

Authors

Williams, S.J.,Ericsson, D.J.,Kobe, B. (deposition date: 2016-07-12, release date: 2017-02-15, Last modification date: 2024-10-30)

Primary citation

Williams, S.J.,Yin, L.,Foley, G.,Casey, L.W.,Outram, M.A.,Ericsson, D.J.,Lu, J.,Boden, M.,Dry, I.B.,Kobe, B.
Structure and Function of the TIR Domain from the Grape NLR Protein RPV1.
Front Plant Sci, 7:1850-1850, 2016

PubMed Abstract: The N-terminal Toll/interleukin-1 receptor/resistance protein (TIR) domain has been shown to be both necessary and sufficient for defense signaling in the model plants flax and . In examples from these organisms, TIR domain self-association is required for signaling function, albeit through distinct interfaces. Here, we investigate these properties in the TIR domain containing resistance protein RPV1 from the wild grapevine . The RPV1 TIR domain, without additional flanking sequence present, is autoactive when transiently expressed in tobacco, demonstrating that the TIR domain alone is capable of cell-death signaling. We determined the crystal structure of the RPV1 TIR domain at 2.3 Å resolution. In the crystals, the RPV1 TIR domain forms a dimer, mediated predominantly through residues in the αA and αE helices ("AE" interface). This interface is shared with the interface discovered in the dimeric complex of the TIR domains from the RPS4/RRS1 resistance protein pair. We show that surface-exposed residues in the AE interface that mediate the dimer interaction in the crystals are highly conserved among plant TIR domain-containing proteins. While we were unable to demonstrate self-association of the RPV1 TIR domain in solution or using yeast 2-hybrid, mutations of surface-exposed residues in the AE interface prevent the cell-death autoactive phenotype. In addition, mutation of residues known to be important in the cell-death signaling function of the flax L6 TIR domain were also shown to be required for RPV1 TIR domain mediated cell-death. Our data demonstrate that multiple TIR domain surfaces control the cell-death function of the RPV1 TIR domain and we suggest that the conserved AE interface may have a general function in TIR-NLR signaling.

PubMed: 28008335
DOI: 10.3389/fpls.2016.01850

Experimental method

X-RAY DIFFRACTION (2.3 Å)