5A31

Structure of the human APC-Cdh1-Hsl1-UbcH10 complex.

Summary for 5A31

• Entry DOI: 10.2210/pdb5a31/pdb
• EMDB information: 2925
• Descriptor: ANAPHASE-PROMOTING COMPLEX SUBUNIT 1, ANAPHASE-PROMOTING COMPLEX SUBUNIT 6, ANAPHASE-PROMOTING COMPLEX SUBUNIT 10, ... (21 entities in total)
• Functional Keywords: ubiquitination, cell cycle, apc/c
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 24
• Total formula weight: 1166487.01

Authors

Chang, L.,Zhang, Z.,Yang, J.,Mclaughlin, S.H.,Barford, D. (deposition date: 2015-05-26, release date: 2015-11-18, Last modification date: 2024-05-08)

Primary citation

Chang, L.,Zhang, Z.,Yang, J.,Mclaughlin, S.H.,Barford, D.
Atomic Structure of the Apc/C and its Mechanism of Protein Ubiquitination.
Nature, 522:450-, 2015

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

Experimental method

ELECTRON MICROSCOPY (4.3 Å)