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TitleMechanism of Lys6 poly-ubiquitin specificity by the L. pneumophila deubiquitinase LotA.
Journal, issue, pagesMol. Cell, Vol. 83, Page 105-120.e5, Year 2023
Publish dateMay 6, 2022 (structure data deposition date)
AuthorsWarren, G.D. / Kitao, T. / Franklin, T.G. / Nguyen, J.V. / Geurink, P.P. / Kubori, T. / Nagai, H. / Pruneda, J.N.
External linksMol. Cell / PubMed:36538933
MethodsX-ray diffraction
Resolution1.5 - 2.8 Å
Structure data

PDB-7uyg:
Structure of the first OTU domain from Legionella pneumophila effector protein LotA
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-7uyh:
Structure of the first OTU domain from Legionella pneumophila effector protein LotA bound to K6-linked diUb
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-IOD:
IODIDE ION

ChemComp-HOH:
WATER

Source
  • legionella pneumophila (bacteria)
  • homo sapiens (human)
KeywordsHYDROLASE / Deubiquitinase / OTU

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