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Structure paper

TitleStructural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34.
Journal, issue, pagesNat Commun, Vol. 10, Page 3296-3296, Year 2019
Publish dateFeb 11, 2019 (structure data deposition date)
AuthorsWilliams, K.M. / Qie, S. / Atkison, J.H. / Salazar-Arango, S. / Alan Diehl, J. / Olsen, S.K.
External linksNat Commun / PubMed:31341161
MethodsX-ray diffraction
Resolution1.502 - 2.065 Å
Structure data

PDB-6nya:
Crystal Structure of ubiquitin E1 (Uba1) in complex with Ubc3 (Cdc34) and ubiquitin
Method: X-RAY DIFFRACTION / Resolution: 2.065 Å

PDB-6nyd:
Crystal Structure of S. cerevisiae Ubc3 (Cdc34)
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-6nyo:
Crystal structure of a human Cdc34-ubiquitin thioester mimetic
Method: X-RAY DIFFRACTION / Resolution: 1.502 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-ACT:
ACETATE ION

ChemComp-U94:
4,5-dideoxy-5-(3',5'-dichlorobiphenyl-4-yl)-4-[(methoxyacetyl)amino]-L-arabinonic acid

ChemComp-PO4:
PHOSPHATE ION

Source
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • triticum aestivum (bread wheat)
  • homo sapiens (human)
  • schizosaccharomyces pombe (fission yeast)
KeywordsLIGASE/TRANSFERASE / CONFORMATIONAL CHANGE / THIOESTER / ADENYLATION / THIOESTER TRANSFER / TRANSTHIOESTERIFICATION / ATP-BINDING / UBIQUITIN E2-BINDING / UBIQUITINATION / LIGASE / LIGASE-TRANSFERASE complex

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