6o0w

Crystal structure of the TIR domain from the grapevine disease resistance protein RUN1 in complex with NADP+ and Bis-Tris

spinqualitylabelsall models 6o0w, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6o0w is a 1 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 1.75Å Ligands: A2P, BTB Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RUN1_VITRO Disease resistance (R) protein that confers resistance to multiple powdery and downy mildew by promoting cell death (PubMed:24033846, PubMed:31439792). 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). Also able to hydrolyze NADP(+), but not other NAD(+)-related molecules (PubMed:31439792). Publication Abstract from PubMed SARM1 (sterile alpha and TIR motif containing 1) is responsible for depletion of nicotinamide adenine dinucleotide in its oxidized form (NAD(+)) during Wallerian degeneration associated with neuropathies. Plant nucleotide-binding leucine-rich repeat (NLR) immune receptors recognize pathogen effector proteins and trigger localized cell death to restrict pathogen infection. Both processes depend on closely related Toll/interleukin-1 receptor (TIR) domains in these proteins, which, as we show, feature self-association-dependent NAD(+) cleavage activity associated with cell death signaling. We further show that SARM1 SAM (sterile alpha motif) domains form an octamer essential for axon degeneration that contributes to TIR domain enzymatic activity. The crystal structures of ribose and NADP(+) (the oxidized form of nicotinamide adenine dinucleotide phosphate) complexes of SARM1 and plant NLR RUN1 TIR domains, respectively, reveal a conserved substrate binding site. NAD(+) cleavage by TIR domains is therefore a conserved feature of animal and plant cell death signaling pathways. NAD(+) cleavage activity by animal and plant TIR domains in cell death pathways.,Horsefield S, Burdett H, Zhang X, Manik MK, Shi Y, Chen J, Qi T, Gilley J, Lai JS, Rank MX, Casey LW, Gu W, Ericsson DJ, Foley G, Hughes RO, Bosanac T, von Itzstein M, Rathjen JP, Nanson JD, Boden M, Dry IB, Williams SJ, Staskawicz BJ, Coleman MP, Ve T, Dodds PN, Kobe B Science. 2019 Aug 23;365(6455):793-799. doi: 10.1126/science.aax1911. PMID:31439792 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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