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Structure paper

TitleStructural and Biochemical Study of the Mono-ADP-Ribosyltransferase Domain of SdeA, a Ubiquitylating/Deubiquitylating Enzyme from Legionella pneumophila
Journal, issue, pagesJ. Mol. Biol., Vol. 430, Page 2843-2856, Year 2018
Publish dateNov 14, 2017 (structure data deposition date)
AuthorsKim, L. / Kwon, D.H. / Kim, B.H. / Kim, J. / Park, M.R. / Park, Z.Y. / Song, H.K.
External linksJ. Mol. Biol. / PubMed:29870726
MethodsX-ray diffraction
Resolution1.546 - 2.403 Å
Structure data

PDB-5ysi:
SdeA mART-C domain EE/AA NCA complex
Method: X-RAY DIFFRACTION / Resolution: 1.546 Å

PDB-5ysj:
SdeA mART-C domain WT apo
Method: X-RAY DIFFRACTION / Resolution: 2.059 Å

PDB-5ysk:
SdeA mART-C domain EE/AA apo
Method: X-RAY DIFFRACTION / Resolution: 2.403 Å

Chemicals

ChemComp-NCA:
NICOTINAMIDE / medication*YM

ChemComp-HOH:
WATER

Source
  • legionella pneumophila subsp. pneumophila str. philadelphia 1 (bacteria)
  • legionella pneumophila subsp. pneumophila (bacteria)
KeywordsHYDROLASE / SdeA / E3 ligase / Legionella

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