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Structure paper

TitleN-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex.
Journal, issue, pagesScience, Vol. 334, Page 674-678, Year 2011
Publish dateAug 11, 2011 (structure data deposition date)
AuthorsScott, D.C. / Monda, J.K. / Bennett, E.J. / Harper, J.W. / Schulman, B.A.
External linksScience / PubMed:21940857
MethodsX-ray diffraction
Resolution1.5 - 2.3 Å
Structure data

PDB-3tdi:
yeast Cul1WHB-Dcn1P acetylated Ubc12N complex
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-3tdu:
N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: Structure of a human Cul1WHB-Dcn1P-acetylated Ubc12N complex
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-3tdz:
N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: Structure of a human Cul1WHB-Dcn1P-stapled acetylated Ubc12N complex
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • homo sapiens (human)
KeywordsLigase/protein binding / E2:E3 / Ligase-protein binding complex / PROTEIN BINDING/INHIBITOR / PROTEIN BINDING-INHIBITOR complex

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