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TitleMolecular architecture and mechanism of the anaphase-promoting complex.
Journal, issue, pagesNature, Vol. 513, Issue 7518, Page 388-393, Year 2014
Publish dateSep 18, 2014
AuthorsLei-Fu Chang / Ziguo Zhang / Jing Yang / Stephen H McLaughlin / David Barford /
PubMed AbstractThe ubiquitination of cell cycle regulatory proteins by the anaphase-promoting complex/cyclosome (APC/C) controls sister chromatid segregation, cytokinesis and the establishment of the G1 phase of ...The ubiquitination of cell cycle regulatory proteins by the anaphase-promoting complex/cyclosome (APC/C) controls sister chromatid segregation, cytokinesis and the establishment of the G1 phase of the cell cycle. The APC/C is an unusually large multimeric cullin-RING ligase. Its activity is strictly dependent on regulatory coactivator subunits that promote APC/C-substrate interactions and stimulate its catalytic reaction. Because the structures of many APC/C subunits and their organization within the assembly are unknown, the molecular basis for these processes is poorly understood. Here, from a cryo-electron microscopy reconstruction of a human APC/C-coactivator-substrate complex at 7.4 Å resolution, we have determined the complete secondary structural architecture of the complex. With this information we identified protein folds for structurally uncharacterized subunits, and the definitive location of all 20 APC/C subunits within the 1.2 MDa assembly. Comparison with apo APC/C shows that the coactivator promotes a profound allosteric transition involving displacement of the cullin-RING catalytic subunits relative to the degron-recognition module of coactivator and APC10. This transition is accompanied by increased flexibility of the cullin-RING subunits and enhanced affinity for UBCH10-ubiquitin, changes which may contribute to coactivator-mediated stimulation of APC/C E3 ligase activity.
External linksNature / PubMed:25043029 / PubMed Central
MethodsEM (single particle)
Resolution7.4 - 9.6 Å
Structure data

EMDB-2651:
Cryo-EM structure of human APC/C-Cdh1-Hsl1 complex at 7.4 A resolution
Method: EM (single particle) / Resolution: 7.4 Å

EMDB-2652:
Cryo-EM structure of human APC/C at 8.7 A resolution
Method: EM (single particle) / Resolution: 8.7 Å

EMDB-2653:
Cryo-EM structure of human APC/C (Apc11-RING deletion) at 8.0 A resolution
Method: EM (single particle) / Resolution: 8.0 Å

EMDB-2654:
Cryo-EM structure of human APC/C (Apc15 deletion) at 9.6 A resolution
Method: EM (single particle) / Resolution: 9.6 Å

Source
  • Homo sapiens (human)

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