title: Structural analysis sheds light on APC/C-mediated ubiquitylation.
abstract: In the December 22nd issue of Molecular Cell, two groups report refined cryo-electron microscopic structures of the APC/C at approximately 20 A resolution. They also reveal important new features including multiple copies of subunits, dimerization and structural flexibility of the APC/C, which give a hint to solve the mechanisms of the APC/C-dependent ubiquitylation.
authors.affiliation: Marie Curie Research Institute, The Chart, Oxted, Surrey, RH8 0TL, United Kingdom.
authors.forename: Yuu
authors.initials: Y
authors.lastname: Kimata
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Yamano
mesh_terms: D064173:Anaphase-Promoting Complex-Cyclosome; D000818:Animals; D006801:Humans; D025821:Polyubiquitin / Q000378:metabolism*; D020836:Protein Structure, Quaternary; D043743:Ubiquitin-Protein Ligase Complexes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D025821:Polyubiquitin; D043743:Ubiquitin-Protein Ligase Complexes; D064173:Anaphase-Promoting Complex-Cyclosome