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TitleCrystal structures of an E1-E2-ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification.
Journal, issue, pagesNat Commun, Vol. 12, Page 2370-2370, Year 2021
Publish dateSep 16, 2020 (structure data deposition date)
AuthorsYuan, L. / Lv, Z. / Adams, M.J. / Olsen, S.K.
External linksNat Commun / PubMed:33888705
MethodsX-ray diffraction
Resolution3.42 Å
Structure data

PDB-7k5j:
Structure of an E1-E2-ubiquitin thioester mimetic
Method: X-RAY DIFFRACTION / Resolution: 3.42 Å

Chemicals

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

Source
  • triticum aestivum (bread wheat)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsSIGNALING PROTEIN / CONFORMATIONAL CHANGE / ADENYLATION / THIOESTER TRANSFER / TRANSTHIOESTERIFICATION / ATP-BINDING / UBIQUITIN E2-BINDING / UBIQUITINATION

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