5ku7

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

spinqualitylabelsall models 5ku7, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ku7 is a 2 chain structure with sequence from Vitis rotundifolia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: MLA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RPV1_VITRO Disease resistance (R) protein that confers resistance to multiple powdery and downy mildew by promoting cell death (PubMed:24033846, PubMed:28008335). Acts as a NAD(+) hydrolase (NADase): in response to activation, catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage triggering a defense system that promotes cell death (PubMed:31439792). Publication Abstract from PubMed 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 Arabidopsis. 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 Muscadinia rotundifolia. 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 A resolution. In the crystals, the RPV1 TIR domain forms a dimer, mediated predominantly through residues in the alphaA and alphaE helices ("AE" interface). This interface is shared with the interface discovered in the dimeric complex of the TIR domains from the Arabidopsis 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. Structure and Function of the TIR Domain from the Grape NLR Protein RPV1.,Williams SJ, Yin L, Foley G, Casey LW, Outram MA, Ericsson DJ, Lu J, Boden M, Dry IB, Kobe B Front Plant Sci. 2016 Dec 8;7:1850. doi: 10.3389/fpls.2016.01850. eCollection, 2016. PMID:28008335 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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