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Structure paper

TitleStructural basis of ubiquitin modification by the Legionella effector SdeA.
Journal, issue, pagesNature, Vol. 557, Page 674-678, Year 2018
Publish dateOct 5, 2017 (structure data deposition date)
AuthorsDong, Y. / Mu, Y. / Xie, Y. / Zhang, Y. / Han, Y. / Zhou, Y. / Wang, W. / Liu, Z. / Wu, M. / Wang, H. ...Dong, Y. / Mu, Y. / Xie, Y. / Zhang, Y. / Han, Y. / Zhou, Y. / Wang, W. / Liu, Z. / Wu, M. / Wang, H. / Pan, M. / Xu, N. / Xu, C.Q. / Yang, M. / Fan, S. / Deng, H. / Tan, T. / Liu, X. / Liu, L. / Li, J. / Wang, J. / Fang, X. / Feng, Y.
External linksNature / PubMed:29795342
MethodsX-ray diffraction
Resolution3.102 - 3.394 Å
Structure data

PDB-5yij:
Structure of a Legionella effector with substrates
Method: X-RAY DIFFRACTION / Resolution: 3.18 Å

PDB-5yik:
Structure of a Legionella effector with its substrate
Method: X-RAY DIFFRACTION / Resolution: 3.102 Å

PDB-5yim:
Structure of a Legionella effector
Method: X-RAY DIFFRACTION / Resolution: 3.394 Å

Chemicals

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

Source
  • legionella pneumophila (bacteria)
  • homo sapiens (human)
KeywordsTRANSFERASE/PROTEIN BINDING / transferase / complex / alpha-helical domain / TRANSFERASE-PROTEIN BINDING complex / monomer / multi-domain protein

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