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PDBsum entry 4ui9
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Contents |
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1441 a.a.
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84 a.a.
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524 a.a.
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55 a.a.
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56 a.a.
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498 a.a.
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25 a.a.
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730 a.a.
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504 a.a.
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182 a.a.
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59 a.a.
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631 a.a.
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685 a.a.
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491 a.a.
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387 a.a.
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94 a.a.
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21 a.a.
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24 a.a.
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25 a.a.
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484 a.a.
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References listed in PDB file
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Key reference
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Title
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Atomic structure of the apc/c and its mechanism of protein ubiquitination.
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Authors
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L.Chang,
Z.Zhang,
J.Yang,
S.H.Mclaughlin,
D.Barford.
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Ref.
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Nature, 2015,
522,
450-454.
[DOI no: ]
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PubMed id
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Abstract
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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.
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