7P8K

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

Summary for 7P8K

• Entry DOI: 10.2210/pdb7p8k/pdb
• Descriptor: Disease resistance protein RRS1, Avirulence protein,Avirulence protein, ZINC ION, ... (4 entities in total)
• Functional Keywords: type iii secreted effector, nlr, integrated domain, transcription
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Total number of polymer chains: 2
• Total formula weight: 19457.14

Authors

Mukhi, N.,Brown, H.,Gorenkin, D.,Ding, P.,Bentham, A.R.,Jones, J.D.G.,Banfield, M.J. (deposition date: 2021-07-23, release date: 2021-08-04, Last modification date: 2024-01-31)

Primary citation

Mukhi, N.,Brown, H.,Gorenkin, D.,Ding, P.,Bentham, A.R.,Stevenson, C.E.M.,Jones, J.D.G.,Banfield, M.J.
Perception of structurally distinct effectors by the integrated WRKY domain of a plant immune receptor.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: Plants use intracellular nucleotide-binding domain (NBD) and leucine-rich repeat (LRR)-containing immune receptors (NLRs) to detect pathogen-derived effector proteins. The NLR pair RRS1-R/RPS4 confers disease resistance to different bacterial pathogens by perceiving the structurally distinct effectors AvrRps4 from pv. and PopP2 from via an integrated WRKY domain in RRS1-R. How the WRKY domain of RRS1 (RRS1) 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) in complex with RRS1 Perception of AvrRps4 by RRS1 is mediated by the β2-β3 segment of RRS1 that binds an electronegative patch on the surface of AvrRps4 Structure-based mutations that disrupt AvrRps4-RRS1 interactions in vitro compromise RRS1/RPS4-dependent immune responses. We also show that AvrRps4 can associate with the WRKY domain of the related but distinct RRS1B/RPS4B NLR pair, and the DNA-binding domain of WRKY41, 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.

PubMed: 34880132
DOI: 10.1073/pnas.2113996118

Experimental method

X-RAY DIFFRACTION (2.65 Å)