5t09 | pdb_00005t09

The structure of the type III effector HopBA1

spinqualitylabelsall models 5t09, resolution 2.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5t09 is a 1 chain structure with sequence from Pseudomonas syringae pv. aptata. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.013Å Ligands: CL, K, MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HPBA1_PSEAP Virulence factor recognized by the A.thaliana disease resistance protein RBA1, which triggers plant cell death (PubMed:28137883). HopBA1 enhances RBA1 self-association, which is necessary for ectopic autoactivation of host cell death (PubMed:28137883). Publication Abstract from PubMed Detection of pathogens by plants is mediated by intracellular nucleotide-binding site leucine-rich repeat (NLR) receptor proteins. NLR proteins are defined by their stereotypical multidomain structure: an N-terminal Toll-interleukin receptor (TIR) or coiled-coil (CC) domain, a central nucleotide-binding (NB) domain, and a C-terminal leucine-rich repeat (LRR). The plant innate immune system contains a limited NLR repertoire that functions to recognize all potential pathogens. We isolated Response to the bacterial type III effector protein HopBA1 (RBA1), a gene that encodes a TIR-only protein lacking all other canonical NLR domains. RBA1 is sufficient to trigger cell death in response to HopBA1. We generated a crystal structure for HopBA1 and found that it has similarity to a class of proteins that includes esterases, the heme-binding protein ChaN, and an uncharacterized domain of Pasteurella multocida toxin. Self-association, coimmunoprecipitation with HopBA1, and function of RBA1 require two previously identified TIR-TIR dimerization interfaces. Although previously described as distinct in other TIR proteins, in RBA1 neither of these interfaces is sufficient when the other is disrupted. These data suggest that oligomerization of RBA1 is required for function. Our identification of RBA1 demonstrates that "truncated" NLRs can function as pathogen sensors, expanding our understanding of both receptor architecture and the mechanism of activation in the plant immune system. TIR-only protein RBA1 recognizes a pathogen effector to regulate cell death in Arabidopsis.,Nishimura MT, Anderson RG, Cherkis KA, Law TF, Liu QL, Machius M, Nimchuk ZL, Yang L, Chung EH, El Kasmi F, Hyunh M, Osborne Nishimura E, Sondek JE, Dangl JL Proc Natl Acad Sci U S A. 2017 Jan 30. pii: 201620973. doi:, 10.1073/pnas.1620973114. PMID:28137883 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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