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TitleS. pombe Uba1-Ubc15 Structure Reveals a Novel Regulatory Mechanism of Ubiquitin E2 Activity.
Journal, issue, pagesMol. Cell, Vol. 65, Page 699-714.e6, Year 2017
Publish dateJun 28, 2016 (structure data deposition date)
AuthorsLv, Z. / Rickman, K.A. / Yuan, L. / Williams, K. / Selvam, S.P. / Woosley, A.N. / Howe, P.H. / Ogretmen, B. / Smogorzewska, A. / Olsen, S.K.
External linksMol. Cell / PubMed:28162934
MethodsX-ray diffraction
Resolution2.5 Å
Structure data

PDB-5knl:
Crystal structure of S. pombe ubiquitin E1 (Uba1) in complex with Ubc15 and ubiquitin
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • schizosaccharomyces pombe (strain 972 / atcc 24843) (yeast)
  • pseudozyma antarctica (fungus)
KeywordsLIGASE / UBIQUITIN / E1 / E2 / UBA1 / UBC15 / CONFORMATIONAL CHANGE / THIOESTER / ADENYLATION / THIOESTER TRANSFER (TRANSTHIOESTERIFICATION) / ATP-Binding / UBIQUITIN E2 BINDING / UBIQUITINATION

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