7UXU
CryoEM structure of the TIR domain from AbTir in complex with 3AD
Summary for 7UXU
| Entry DOI | 10.2210/pdb7uxu/pdb |
| EMDB information | 26862 |
| Descriptor | Molecular chaperone Tir, [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2~{R},3~{S},4~{R},5~{R})-5-(8-azanylisoquinolin-2-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl hydrogen phosphate (2 entities in total) |
| Functional Keywords | 2' cadpr, nadase, bacterial tir, hydrolase |
| Biological source | Acinetobacter baumannii |
| Total number of polymer chains | 4 |
| Total formula weight | 65204.08 |
| Authors | Li, S.,Nanson, J.D.,Manik, M.K.,Gu, W.,Landsberg, M.J.,Ve, T.,Kobe, B. (deposition date: 2022-05-06, release date: 2022-09-07, Last modification date: 2024-06-12) |
| Primary citation | Manik, M.K.,Shi, Y.,Li, S.,Zaydman, M.A.,Damaraju, N.,Eastman, S.,Smith, T.G.,Gu, W.,Masic, V.,Mosaiab, T.,Weagley, J.S.,Hancock, S.J.,Vasquez, E.,Hartley-Tassell, L.,Kargios, N.,Maruta, N.,Lim, B.Y.J.,Burdett, H.,Landsberg, M.J.,Schembri, M.A.,Prokes, I.,Song, L.,Grant, M.,DiAntonio, A.,Nanson, J.D.,Guo, M.,Milbrandt, J.,Ve, T.,Kobe, B. Cyclic ADP ribose isomers: Production, chemical structures, and immune signaling. Science, 377:eadc8969-eadc8969, 2022 Cited by PubMed Abstract: Cyclic adenosine diphosphate (ADP)-ribose (cADPR) isomers are signaling molecules produced by bacterial and plant Toll/interleukin-1 receptor (TIR) domains via nicotinamide adenine dinucleotide (oxidized form) (NAD) hydrolysis. We show that v-cADPR (2'cADPR) and v2-cADPR (3'cADPR) isomers are cyclized by O-glycosidic bond formation between the ribose moieties in ADPR. Structures of 2'cADPR-producing TIR domains reveal conformational changes that lead to an active assembly that resembles those of Toll-like receptor adaptor TIR domains. Mutagenesis reveals a conserved tryptophan that is essential for cyclization. We show that 3'cADPR is an activator of ThsA effector proteins from the bacterial antiphage defense system termed Thoeris and a suppressor of plant immunity when produced by the effector HopAM1. Collectively, our results reveal the molecular basis of cADPR isomer production and establish 3'cADPR in bacteria as an antiviral and plant immunity-suppressing signaling molecule. PubMed: 36048923DOI: 10.1126/science.adc8969 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.74 Å) |
Structure validation
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