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Structure paper

TitleCyclic ADP ribose isomers: Production, chemical structures, and immune signaling.
Journal, issue, pagesScience, Vol. 377, Issue 6614, Page eadc8969, Year 2022
Publish dateSep 30, 2022
AuthorsMohammad K Manik / Yun Shi / Sulin Li / Mark A Zaydman / Neha Damaraju / Samuel Eastman / Thomas G Smith / Weixi Gu / Veronika Masic / Tamim Mosaiab / James S Weagley / Steven J Hancock / Eduardo Vasquez / Lauren Hartley-Tassell / Nestoras Kargios / Natsumi Maruta / Bryan Y J Lim / Hayden Burdett / Michael J Landsberg / Mark A Schembri / Ivan Prokes / Lijiang Song / Murray Grant / Aaron DiAntonio / Jeffrey D Nanson / Ming Guo / Jeffrey Milbrandt / Thomas Ve / Bostjan Kobe /
PubMed AbstractCyclic adenosine diphosphate (ADP)-ribose (cADPR) isomers are signaling molecules produced by bacterial and plant Toll/interleukin-1 receptor (TIR) domains via nicotinamide adenine dinucleotide ...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.
External linksScience / PubMed:36048923
MethodsEM (helical sym.) / X-ray diffraction
Resolution1.42 - 3.4 Å
Structure data

26862

7uxu

EMDB-26862, PDB-7uxu:
CryoEM structure of the TIR domain from AbTir in complex with 3AD
Method: EM (helical sym.) / Resolution: 2.74 Å

PDB-7uwg:
The crystal structure of the TIR domain-containing protein from Acinetobacter baumannii (AbTir)
Method: X-RAY DIFFRACTION / Resolution: 2.16 Å

PDB-7uxr:
Crystal structure of the BtTir TIR domain
Method: X-RAY DIFFRACTION / Resolution: 1.42 Å

PDB-7uxs:
Crystal structure of the BcThsA SLOG domain in complex with 3'cADPR
Method: X-RAY DIFFRACTION / Resolution: 1.57 Å

PDB-7uxt:
Crystal structure of ligand-free SeThsA
Method: X-RAY DIFFRACTION / Resolution: 3.4 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-P6G:
HEXAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-OJC:
(2R,3R,3aS,5S,6R,7S,8R,11R,13S,15aR)-2-(6-amino-9H-purin-9-yl)-3,6,7,11,13-pentahydroxyoctahydro-2H,5H,11H,13H-5,8-epoxy-11lambda~5~,13lambda~5~-furo[2,3-g][1,3,5,9,2,4]tetraoxadiphosphacyclotetradecine-11,13-dione

ChemComp-GOL:
GLYCEROL

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-1O4:
[[(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

Source
  • acinetobacter baumannii (bacteria)
  • bacteroides thetaiotaomicron (bacteria)
  • bacillus subtilis (bacteria)
  • streptococcus equi (bacteria)
KeywordsHYDROLASE / 2' cADPR / NADase / Bacterial TIR / cADPR isomer / NAD+ / Thoeris defense system / ThsA / ThsB / antiphage defense

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