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PDBsum entry 3m99
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Transcription
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PDB id
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3m99
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Contents |
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422 a.a.
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89 a.a.
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91 a.a.
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84 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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Structural basis for assembly and activation of the heterotetrameric saga histone h2b deubiquitinase module.
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Authors
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A.Köhler,
E.Zimmerman,
M.Schneider,
E.Hurt,
N.Zheng.
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Ref.
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Cell, 2010,
141,
606-617.
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PubMed id
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Abstract
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Deubiquitinating enzymes (DUBs) regulate diverse cellular functions by cleaving
ubiquitin from specific protein substrates. How their activities are modulated
in various cellular contexts remains poorly understood. The yeast deubiquitinase
Ubp8 protein is recruited and activated by the SAGA complex and, together with
Sgf11, Sus1, and Sgf73, forms a DUB module responsible for deubiquitinating
histone H2B during gene expression. Here, we report the crystal structure of the
complete SAGA DUB module, which features two functional lobes structurally
coupled by Sgf73. In the "assembly lobe," a long Sgf11 N-terminal helix is
clamped onto the Ubp8 ZnF-UBP domain by Sus1. In the "catalytic lobe," an Sgf11
C-terminal zinc-finger domain binds to the Ubp8 catalytic domain next to its
active site. Our structural and functional analyses reveal a central role of
Sgf11 and Sgf73 in activating Ubp8 for deubiquitinating histone H2B and
demonstrate how a DUB can be allosterically regulated by its nonsubstrate
partners.
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