7p8k

Crystal structure of in planta processed AvrRps4 in complex with the WRKY domain of RRS1

spinqualitylabelsall models 7p8k, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7p8k is a 2 chain structure with sequence from Arabidopsis thaliana and Pseudomonas syringae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.65Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function WR52W_ARATH Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Acts also as a disease resistance protein involved in resistance to fungal and bacterial pathogens, including R.solanacearum, P.syringae pv. tomato and C.higginsianum. In presence of RPS4, elicites an EDS1-dependent hypersensitive response (PubMed:24146667).[UniProtKB:Q9FH83] Publication Abstract from PubMed Plants use intracellular nucleotide-binding domain (NBD) and leucine-rich repeat (LRR)-containing immune receptors (NLRs) to detect pathogen-derived effector proteins. The Arabidopsis NLR pair RRS1-R/RPS4 confers disease resistance to different bacterial pathogens by perceiving the structurally distinct effectors AvrRps4 from Pseudomonas syringae pv. pisi and PopP2 from Ralstonia solanacearum via an integrated WRKY domain in RRS1-R. How the WRKY domain of RRS1 (RRS1(WRKY)) perceives distinct classes of effector to initiate an immune response is unknown. Here, we report the crystal structure of the in planta processed C-terminal domain of AvrRps4 (AvrRps4(C)) in complex with RRS1(WRKY) Perception of AvrRps4(C) by RRS1(WRKY) is mediated by the beta2-beta3 segment of RRS1(WRKY) that binds an electronegative patch on the surface of AvrRps4(C) Structure-based mutations that disrupt AvrRps4(C)-RRS1(WRKY) interactions in vitro compromise RRS1/RPS4-dependent immune responses. We also show that AvrRps4(C) can associate with the WRKY domain of the related but distinct RRS1B/RPS4B NLR pair, and the DNA-binding domain of AtWRKY41, with similar binding affinities and how effector binding interferes with WRKY-W-box DNA interactions. This work demonstrates how integrated domains in plant NLRs can directly bind structurally distinct effectors to initiate immunity. Perception of structurally distinct effectors by the integrated WRKY domain of a plant immune receptor.,Mukhi N, Brown H, Gorenkin D, Ding P, Bentham AR, Stevenson CEM, Jones JDG, Banfield MJ Proc Natl Acad Sci U S A. 2021 Dec 14;118(50):e2113996118. doi: , 10.1073/pnas.2113996118. PMID:34880132 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Avirulence protein 3D structures

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