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4UI9

Atomic structure of the human Anaphase-Promoting Complex

Summary for 4UI9
Entry DOI10.2210/pdb4ui9/pdb
EMDB information2924
DescriptorANAPHASE-PROMOTING COMPLEX SUBUNIT 1, CELL DIVISION CYCLE PROTEIN 16 HOMOLOG, ANAPHASE-PROMOTING COMPLEX SUBUNIT 10, ... (21 entities in total)
Functional Keywordsubiquitination, cell cycle, apc/c, apc subunits, anaphase promoting complex
Biological sourceHOMO SAPIENS (HUMAN)
More
Total number of polymer chains23
Total formula weight1272960.77
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 citationChang, 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: 26083744
DOI: 10.1038/NATURE14471
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

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