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PDBsum entry 4r8p
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Structural protein/DNA
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PDB id
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4r8p
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Contents |
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98 a.a.
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86 a.a.
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104 a.a.
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95 a.a.
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105 a.a.
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254 a.a.
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97 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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Crystal structure of the prc1 ubiquitylation module bound to the nucleosome.
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Authors
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R.K.Mcginty,
R.C.Henrici,
S.Tan.
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Ref.
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Nature, 2014,
514,
591-596.
[DOI no: ]
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PubMed id
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Abstract
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The Polycomb group of epigenetic enzymes represses expression of developmentally
regulated genes in many eukaryotes. This group includes the Polycomb repressive
complex 1 (PRC1), which ubiquitylates nucleosomal histone H2A Lys 119 using its
E3 ubiquitin ligase subunits, Ring1B and Bmi1, together with an E2
ubiquitin-conjugating enzyme, UbcH5c. However, the molecular mechanism of
nucleosome substrate recognition by PRC1 or other chromatin enzymes is unclear.
Here we present the crystal structure of the human Ring1B-Bmi1-UbcH5c E3-E2
complex (the PRC1 ubiquitylation module) bound to its nucleosome core particle
substrate. The structure shows how a chromatin enzyme achieves substrate
specificity by interacting with several nucleosome surfaces spatially distinct
from the site of catalysis. Our structure further reveals an unexpected role for
the ubiquitin E2 enzyme in substrate recognition, and provides insight into how
the related histone H2A E3 ligase, BRCA1, interacts with and ubiquitylates the
nucleosome.
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