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TitleThe RBR E3 ubiquitin ligase HOIL-1 can ubiquitinate diverse non-protein substrates in vitro.
Journal, issue, pagesLife Sci Alliance, Vol. 8, Year 2025
Publish dateNov 21, 2024 (structure data deposition date)
AuthorsWang, X.S. / Jiou, J. / Cerra, A. / Cobbold, S.A. / Jochem, M. / Mak, K.H.T. / Corcilius, L. / Silke, J. / Payne, R.J. / Goddard-Borger, E.D. ...Wang, X.S. / Jiou, J. / Cerra, A. / Cobbold, S.A. / Jochem, M. / Mak, K.H.T. / Corcilius, L. / Silke, J. / Payne, R.J. / Goddard-Borger, E.D. / Komander, D. / Lechtenberg, B.C.
External linksLife Sci Alliance / PubMed:40169258
MethodsX-ray diffraction
Resolution1.78 - 2 Å
Structure data

PDB-9egv:
HOIL-1 RING2 domain bound to ubiquitin
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-9egw:
HOIL-1 RING2 domain bound to ubiquitin-maltose (maltose not modelled)
Method: X-RAY DIFFRACTION / Resolution: 1.78 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsLIGASE / RBR E3 ubiquitin ligase / enzyme-substrate complex / RING2 domain

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