7xdd | pdb_00007xdd

Cryo-EM structure of EDS1 and PAD4

spinqualitylabelsall models 7xdd, resolution 2.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7xdd is a 2 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PAD4_ARATH] Probable lipase required downstream of MPK4 for accumulation of the plant defense-potentiating molecule, salicylic acid, thus contributing to the plant innate immunity against invasive biotrophic pathogens and to defense mechanisms upon recognition of microbe-associated molecular patterns (MAMPs). Participates in the regulation of various molecular and physiological processes that influence fitness. Together with SG101, required for programmed cell death (PCD) triggered by NBS-LRR resistance proteins (e.g. RPS4, RPW8.1 and RPW8.2) in response to the fungal toxin fumonisin B1 (FB1) and avirulent pathogens (e.g. P.syringae pv. tomato strain DC3000 avrRps4 and pv. maculicola, turnip crinkle virus (TCV), and H.arabidopsidis isolates CALA2, EMOY2, EMWA1 and HIND4). Together with EDS1, confers a basal resistance by restricting the growth of virulent pathogens (e.g. H.arabidopsidis isolates NOCO2 and EMCO5, E.orontii isolate MGH, and P.syringae pv. tomato strain DC3000 or expressing HopW1-1 (HopPmaA)). Necessary for the salicylic acid-(SA-) dependent systemic acquired resistance (SAR) response that involves expression of multiple defense responses, including synthesis of the phytoalexin camalexin and expression of pathogenesis-related genes (e.g. PR1, ALD1, BGL2 and PR5) in response to pathogens, triggering a signal amplification loop that increases SA levels via EDS5 and SID2, but, together with EDS1, seems to repress the ethylene/jasmonic acid (ET/JA) defense pathway. May also function in response to abiotic stresses such as UV-C light and LSD1-dependent acclimatization to light conditions that promote excess excitation energy (EEE), probably by transducing redox signals and modulating stomatal conductance. Regulates the formation of lysigenous aerenchyma in hypocotyls in response to hypoxia, maybe via hydrogen peroxide production. Modulates leaf senescence in insect-infested tissue and triggers a phloem-based defense mechanism including antibiosis (e.g. green peach aphid (GPA), M.persicae) to limit phloem sap uptake and insect growth, thus providing an EDS1-independent basal resistance to insects. Also involved in regulation of root meristematic zone-targeted growth arrest together with EDS1 and in a VICTR-dependent manner. Publication Abstract from PubMed Plant nucleotide-binding leucine-rich repeat-containing (NLR) receptors with an N-terminal Toll/interleukin-1 receptor (TIR) domain sense pathogen effectors to enable TIR-encoded nicotinamide adenine dinucleotide hydrolase (NADase) activity for immune signaling. TIR-NLR signaling requires the helper NLRs N requirement gene 1 (NRG1), Activated Disease Resistance 1 (ADR1), and Enhanced Disease Susceptibility 1 (EDS1), which forms a heterodimer with each of its paralogs Phytoalexin Deficient 4 (PAD4) and Senescence-Associated Gene 101 (SAG101). Here, we show that TIR-containing proteins catalyze the production of 2'-(5-phosphoribosyl)-5'-adenosine monophosphate (pRib-AMP) and diphosphate (pRib-ADP) in vitro and in planta. Biochemical and structural data demonstrate that EDS1-PAD4 is a receptor complex for pRib-AMP and pRib-ADP, which allosterically promote EDS1-PAD4 interaction with ADR1-L1 but not NRG1A. Our study identifies TIR-catalyzed pRib-AMP and pRib-ADP as a missing link in TIR signaling through EDS1-PAD4 and as likely second messengers for plant immunity. Identification and receptor mechanism of TIR-catalyzed small molecules in plant immunity.,Huang S, Jia A, Song W, Hessler G, Meng Y, Sun Y, Xu L, Laessle H, Jirschitzka J, Ma S, Xiao Y, Yu D, Hou J, Liu R, Sun H, Liu X, Han Z, Chang J, Parker JE, Chai J Science. 2022 Jul 29;377(6605):eabq3297. doi: 10.1126/science.abq3297. Epub 2022 , Jul 29. PMID:35857645 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA