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TitleA Structurally Unique E2-Binding Domain Activates Ubiquitination by the ERAD E2, Ubc7p, through Multiple Mechanisms.
Journal, issue, pagesMol. Cell, Vol. 50, Page 516-527, Year 2013
Publish dateMar 20, 2013 (structure data deposition date)
AuthorsMetzger, M.B. / Liang, Y.H. / Das, R. / Mariano, J. / Li, S. / Li, J. / Kostova, Z. / Byrd, R.A. / Ji, X. / Weissman, A.M.
External linksMol. Cell / PubMed:23665230
MethodsX-ray diffraction
Resolution1.81 Å
Structure data

PDB-4jqu:
Crystal structure of Ubc7p in complex with the U7BR of Cue1p
Method: X-RAY DIFFRACTION / Resolution: 1.81 Å

Chemicals

ChemComp-BTB:
2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsLIGASE/PROTEIN BINDING / Ubc7p:U7BR complex / ligase-activator complex / LIGASE-PROTEIN BINDING complex

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