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TitleStructures of APC/C(Cdh1) with substrates identify Cdh1 and Apc10 as the D-box co-receptor.
Journal, issue, pagesNature, Vol. 470, Issue 7333, Page 274-278, Year 2011
Publish dateFeb 10, 2011
AuthorsPaula C A da Fonseca / Eric H Kong / Ziguo Zhang / Anne Schreiber / Mark A Williams / Edward P Morris / David Barford /
PubMed AbstractThe ubiquitylation of cell-cycle regulatory proteins by the large multimeric anaphase-promoting complex (APC/C) controls sister chromatid segregation and the exit from mitosis. Selection of APC/C ...The ubiquitylation of cell-cycle regulatory proteins by the large multimeric anaphase-promoting complex (APC/C) controls sister chromatid segregation and the exit from mitosis. Selection of APC/C targets is achieved through recognition of destruction motifs, predominantly the destruction (D)-box and KEN (Lys-Glu-Asn)-box. Although this process is known to involve a co-activator protein (either Cdc20 or Cdh1) together with core APC/C subunits, the structural basis for substrate recognition and ubiquitylation is not understood. Here we investigate budding yeast APC/C using single-particle electron microscopy and determine a cryo-electron microscopy map of APC/C in complex with the Cdh1 co-activator protein (APC/C(Cdh1)) bound to a D-box peptide at ∼10 Å resolution. We find that a combined catalytic and substrate-recognition module is located within the central cavity of the APC/C assembled from Cdh1, Apc10--a core APC/C subunit previously implicated in substrate recognition--and the cullin domain of Apc2. Cdh1 and Apc10, identified from difference maps, create a co-receptor for the D-box following repositioning of Cdh1 towards Apc10. Using NMR spectroscopy we demonstrate specific D-box-Apc10 interactions, consistent with a role for Apc10 in directly contributing towards D-box recognition by the APC/C(Cdh1) complex. Our results rationalize the contribution of both co-activator and core APC/C subunits to D-box recognition and provide a structural framework for understanding mechanisms of substrate recognition and catalysis by the APC/C.
External linksNature / PubMed:21107322 / PubMed Central
MethodsEM (single particle)
Resolution11.0 - 20.0 Å
Structure data

EMDB-1815:
The structure of anaphase promoting complex-Cdh1-Dbox at 10 Angstroms resolution
Method: EM (single particle) / Resolution: 11.0 Å

EMDB-1816:
Structure of S. cerevisiae anaphase promoting complex
Method: EM (single particle)

EMDB-1817:
Structure of S. cerevisiae anaphase promoting complex with the co-activator Cdh1
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-1818:
Structure of S. cerevisiae anaphase promoting complex-Cdh1-KENbox peptide
Method: EM (single particle)

EMDB-1819:
Structure of S. cerevisiae anaphase promoting complex-Cdh1 bound to a Hsl1 fragment
Method: EM (single particle)

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • synthetic construct (others)

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