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TitleCryo-EM structures of apo-APC/C and APC/C complexes provide insights into APC/C regulation.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 10074, Year 2024
Publish dateNov 21, 2024
AuthorsAnna Höfler / Jun Yu / Jing Yang / Ziguo Zhang / Leifu Chang / Stephen H McLaughlin / Geoffrey W Grime / Elspeth F Garman / Andreas Boland / David Barford /
PubMed AbstractAPC/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 ...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.
External linksNat Commun / PubMed:39567505 / PubMed Central
MethodsEM (single particle)
Resolution2.85 - 3.2 Å
Structure data

13931

9gaw

EMDB-13931, PDB-9gaw:
High-resolution structure of the Anaphase-promoting complex/cyclosome (APC/C) bound to co-activator Cdh1
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-13932:
Focused refined map of the catalytic module of the Anaphase-promoting complex/cyclosome (APC/C).
Method: EM (single particle) / Resolution: 3.17 Å

EMDB-13933:
Focused refined map of the TPR lobe of the Anaphase-promoting complex/cyclosome (APC/C)
Method: EM (single particle) / Resolution: 2.85 Å

17751

8pkp

EMDB-17751, PDB-8pkp:
Cryo-EM structure of the apo Anaphase-promoting complex/cyclosome (APC/C) at 3.2 Angstrom resolution
Method: EM (single particle) / Resolution: 3.2 Å

19711

9gaw

EMDB-19711: Cryo-EM structure of the Anaphase-promoting complex/cyclosome (APC/C) bound to co-activator Cdh1 at 3.2 Angstrom resolution
PDB-9gaw: High-resolution structure of the Anaphase-promoting complex/cyclosome (APC/C) bound to co-activator Cdh1
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-51070: Focused refined map of the Anaphase-promoting complex/cyclosome (APC/C) with mask 3
Method: EM (single particle) / Resolution: 3.1 Å

51190

9gaw

EMDB-51190, PDB-9gaw:
High-resolution structure of the Anaphase-promoting complex/cyclosome (APC/C) bound to co-activator Cdh1
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsCELL CYCLE / APC/C / cyclosome / Cdc20 / Cdh1 / ubiquitination / Emi1 / mitosis

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