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TitleSelf-association configures the NAD + -binding site of plant NLR TIR domains
Journal, issue, pagesBiorxiv, Year 2021
Publish dateAug 15, 2021 (structure data deposition date)
AuthorsBurdett, H. / Hu, X. / Rank, M.X. / Maruta, N. / Kobe, B.
External linksBiorxiv / Search PubMed
MethodsX-ray diffraction
Resolution1.74 - 2.35 Å
Structure data

PDB-7rts:
Crystal structure of the TIR domain from the grapevine disease resistance protein RUN1 without the AE interface
Method: X-RAY DIFFRACTION / Resolution: 1.74 Å

PDB-7rx1:
Crystal structure of the TIR domain from the grapevine disease resistance protein RUN1
Method: X-RAY DIFFRACTION / Resolution: 1.89 Å

PDB-7s2z:
Crystal structure of the E100A mutant TIR domain from the grapevine disease resistance protein RUN1 bound to NAD
Method: X-RAY DIFFRACTION / Resolution: 2.35 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

Source
  • vitis rotundifolia (fox grape)
KeywordsSIGNALING PROTEIN / NAD+ Hydrolase / Signalling Protein / TIR domain / NAD+ nucleosidase activity / HYDROLASE

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