Structural organization of the anaphase-promoting complex bound to the mitotic activator Slp1.

Ohi MD, Feoktistova A, Ren L, Yip C, Cheng Y, Chen JS, Yoon HJ, Wall JS, Huang Z, Penczek PA, Gould KL, Walz T
Mol Cell. 2007 28 (5): 871-85

PMID: 18082611 · PMCID: PMC2197158 · DOI:10.1016/j.molcel.2007.10.003

The anaphase-promoting complex/cyclosome (APC/C) is a conserved multisubunit E3 ubiquitin (Ub) ligase required to signal the degradation of key cell-cycle regulators. Using single particle cryo-electron microscopy (cryo-EM), we have determined a three-dimensional (3D) structure of the core APC/C from Schizosaccharomyces pombe bound to the APC/C activator Slp1/Cdc20. At the 27 A resolution of our density map, the APC/C is a triangular-shaped structure, approximately 19x17x15 nm in size, with a deep internal cavity and a prominent horn-like protrusion emanating from a lip of the cavity. Using antibody labeling and mutant analysis, we have localized 12 of 13 core APC/C components, as well as the position of the activator Slp1, enabling us to propose a structural model of APC/C organization. Comparison of the APC/C with another multiprotein E3 ligase, the SCF complex, uncovers remarkable structural similarities.

MeSH Terms (16)

Anaphase-Promoting Complex-Cyclosome Cdc20 Proteins Cell Cycle Proteins Chromatography, Affinity Cryoelectron Microscopy Immunoblotting Mitosis Models, Molecular Mutagenesis, Site-Directed Mutation Protein Conformation Schizosaccharomyces Schizosaccharomyces pombe Proteins Ubiquitin-Protein Ligase Complexes Ubiquitin-Protein Ligases Ubiquitination

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