4UI9
Atomic structure of the human Anaphase-Promoting Complex
Summary for 4UI9
Entry DOI | 10.2210/pdb4ui9/pdb |
EMDB information | 2924 |
Descriptor | ANAPHASE-PROMOTING COMPLEX SUBUNIT 1, CELL DIVISION CYCLE PROTEIN 16 HOMOLOG, ANAPHASE-PROMOTING COMPLEX SUBUNIT 10, ... (21 entities in total) |
Functional Keywords | ubiquitination, cell cycle, apc/c, apc subunits, anaphase promoting complex |
Biological source | HOMO SAPIENS (HUMAN) More |
Total number of polymer chains | 23 |
Total formula weight | 1272960.77 |
Authors | Chang, L.,Zhang, Z.,Yang, J.,McLaughlin, S.H.,Barford, D. (deposition date: 2015-03-27, release date: 2015-06-17, Last modification date: 2024-05-08) |
Primary citation | Chang, L.,Zhang, Z.,Yang, J.,Mclaughlin, S.H.,Barford, D. Atomic Structure of the Apc and its Mechanism of Protein Ubiquitination Nature, 522:450-, 2015 Cited by PubMed Abstract: The anaphase-promoting complex (APC/C) is a multimeric RING E3 ubiquitin ligase that controls chromosome segregation and mitotic exit. Its regulation by coactivator subunits, phosphorylation, the mitotic checkpoint complex and interphase early mitotic inhibitor 1 (Emi1) ensures the correct order and timing of distinct cell-cycle transitions. Here we use cryo-electron microscopy to determine atomic structures of APC/C-coactivator complexes with either Emi1 or a UbcH10-ubiquitin conjugate. These structures define the architecture of all APC/C subunits, the position of the catalytic module and explain how Emi1 mediates inhibition of the two E2s UbcH10 and Ube2S. Definition of Cdh1 interactions with the APC/C indicates how they are antagonized by Cdh1 phosphorylation. The structure of the APC/C with UbcH10-ubiquitin reveals insights into the initiating ubiquitination reaction. Our results provide a quantitative framework for the design of future experiments to investigate APC/C functions in vivo. PubMed: 26083744DOI: 10.1038/NATURE14471 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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