8PKP
Cryo-EM structure of the apo Anaphase-promoting complex/cyclosome (APC/C) at 3.2 Angstrom resolution
Summary for 8PKP
| Entry DOI | 10.2210/pdb8pkp/pdb |
| EMDB information | 13931 17751 3388 |
| Descriptor | Anaphase-promoting complex subunit 1, Cell division cycle protein 23 homolog, Anaphase-promoting complex subunit 7, ... (15 entities in total) |
| Functional Keywords | apc/c, cyclosome, cdc20, cdh1, ubiquitination, emi1, mitosis, cell cycle |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 19 |
| Total formula weight | 1166029.12 |
| Authors | Hoefler, A.,Yu, J.,Chang, L.,Zhang, Z.,Yang, J.,Boland, A.,Barford, D. (deposition date: 2023-06-27, release date: 2023-07-19, Last modification date: 2025-01-29) |
| Primary citation | Hofler, A.,Yu, J.,Yang, J.,Zhang, Z.,Chang, L.,McLaughlin, S.H.,Grime, G.W.,Garman, E.F.,Boland, A.,Barford, D. Cryo-EM structures of apo-APC/C and APC/C CDH1:EMI1 complexes provide insights into APC/C regulation. Nat Commun, 15:10074-10074, 2024 Cited by PubMed Abstract: APC/C is a multi-subunit complex that functions as a master regulator of cell division. It controls progression through the cell cycle by timely marking mitotic cyclins and other cell cycle regulatory proteins for degradation. The APC/C itself is regulated by the sequential action of its coactivator subunits CDC20 and CDH1, post-translational modifications, and its inhibitory binding partners EMI1 and the mitotic checkpoint complex. In this study, we took advantage of developments in cryo-electron microscopy to determine the structures of human APC/C and apo-APC/C at 2.9 Å and 3.2 Å resolution, respectively, providing insights into the regulation of APC/C activity. The high-resolution maps allow the unambiguous assignment of an α-helix to the N-terminus of CDH1 (CDH1) in the APC/C ternary complex. We also identify a zinc-binding module in APC2 that confers structural stability to the complex, and we confirm the presence of zinc ions experimentally. Finally, due to the higher resolution and well defined density of these maps, we are able to build, aided by AlphaFold predictions, several intrinsically disordered regions in different APC/C subunits that likely play a role in proper APC/C assembly and regulation of its activity. PubMed: 39567505DOI: 10.1038/s41467-024-54398-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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