7mk3
Crystal structure of NPR1
Structural highlights
FunctionNPR1_ARATH May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Key positive regulator of the SA-dependent signaling pathway that negatively regulates JA-dependent signaling pathway. Mediates the binding of TGA factors to the as-1 motif found in the pathogenesis-related PR-1 gene, leading to the transcriptional regulation of the gene defense. Controls the onset of systemic acquired resistance (SAR). Upon SAR induction, a biphasic change in cellular reduction potential occurs, resulting in reduction of the cytoplasmic oligomeric form to a monomeric form that accumulates in the nucleus and activates gene expression. Phosphorylated form is target of proteasome degradation.[1] [2] [3] [4] [5] [6] [7] Publication Abstract from PubMedNPR1 is a master regulator of the defence transcriptome induced by the plant immune signal salicylic acid(1-4). Despite the important role of NPR1 in plant immunity(5-7), understanding of its regulatory mechanisms has been hindered by a lack of structural information. Here we report cryo-electron microscopy and crystal structures of Arabidopsis NPR1 and its complex with the transcription factor TGA3. Cryo-electron microscopy analysis reveals that NPR1 is a bird-shaped homodimer comprising a central Broad-complex, Tramtrack and Bric-a-brac (BTB) domain, a BTB and carboxyterminal Kelch helix bundle, four ankyrin repeats and a disordered salicylic-acid-binding domain. Crystal structure analysis reveals a unique zinc-finger motif in BTB for interacting with ankyrin repeats and mediating NPR1 oligomerization. We found that, after stimulation, salicylic-acid-induced folding and docking of the salicylic-acid-binding domain onto ankyrin repeats is required for the transcriptional cofactor activity of NPR1, providing a structural explanation for a direct role of salicylic acid in regulating NPR1-dependent gene expression. Moreover, our structure of the TGA32-NPR12-TGA32 complex, DNA-binding assay and genetic data show that dimeric NPR1 activates transcription by bridging two fatty-acid-bound TGA3 dimers to form an enhanceosome. The stepwise assembly of the NPR1-TGA complex suggests possible hetero-oligomeric complex formation with other transcription factors, revealing how NPR1 reprograms the defence transcriptome. Structural basis of NPR1 in activating plant immunity.,Kumar S, Zavaliev R, Wu Q, Zhou Y, Cheng J, Dillard L, Powers J, Withers J, Zhao J, Guan Z, Borgnia MJ, Bartesaghi A, Dong X, Zhou P Nature. 2022 May;605(7910):561-566. doi: 10.1038/s41586-022-04699-w. Epub 2022, May 11. PMID:35545668[8] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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