The Active Form of E6-associated protein (E6AP)/UBE3A Ubiquitin Ligase Is an Oligomer

• Published in: The Journal of biological chemistry Vol. 289; no. 2; pp. 1033 - 1048
• Main Authors: Ronchi, Virginia P., Klein, Jennifer M., Edwards, Daniel J., Haas, Arthur L.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 10.01.2014; American Society for Biochemistry and Molecular Biology
• Subjects: Amino Acid Sequence; Angelman Syndrome - genetics; Angelman Syndrome - metabolism; Animals; Binding Sites - genetics; Biocatalysis; E3 Ubiquitin Ligase; Electrophoresis, Polyacrylamide Gel; Enzyme Kinetics; Enzyme Mechanisms; Enzymology; Hect Ligase; Humans; Hydrogen Bonding; Iodine Radioisotopes; Isoenzymes - chemistry; Isoenzymes - genetics; Isoenzymes - metabolism; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Phylogeny; Polyubiquitin - metabolism; Protein Multimerization; Protein Structure, Secondary; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Sf9 Cells; Ubiquitin; Ubiquitin - metabolism; Ubiquitin-Protein Ligases - chemistry; Ubiquitin-Protein Ligases - genetics; Ubiquitin-Protein Ligases - metabolism; Enzyme Mechanisms; Ubiquitin; E3 Ubiquitin Ligase; Hect Ligase; Enzyme Kinetics; Kinetics

Employing 125I-polyubiquitin chain formation as a functional readout of ligase activity, biochemical and biophysical evidence demonstrates that catalytically active E6-associated protein (E6AP)/UBE3A is an oligomer. Based on an extant structure previously discounted as an artifact of crystal packing...