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PDBsum entry 3mhh
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Hydrolase/transcription
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PDB id
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3mhh
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Contents |
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433 a.a.
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93 a.a.
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93 a.a.
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92 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 insights into the assembly and function of the saga deubiquitinating module.
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Authors
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N.L.Samara,
A.B.Datta,
C.E.Berndsen,
X.Zhang,
T.Yao,
R.E.Cohen,
C.Wolberger.
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Ref.
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Science, 2010,
328,
1025-1029.
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PubMed id
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Abstract
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SAGA is a transcriptional coactivator complex that is conserved across
eukaryotes and performs multiple functions during transcriptional activation and
elongation. One role is deubiquitination of histone H2B, and this activity
resides in a distinct subcomplex called the deubiquitinating module (DUBm),
which contains the ubiquitin-specific protease Ubp8, bound to Sgf11, Sus1, and
Sgf73. The deubiquitinating activity depends on the presence of all four DUBm
proteins. We report here the 1.90 angstrom resolution crystal structure of the
DUBm bound to ubiquitin aldehyde, as well as the 2.45 angstrom resolution
structure of the uncomplexed DUBm. The structure reveals an arrangement of
protein domains that gives rise to a highly interconnected complex, which is
stabilized by eight structural zinc atoms that are critical for enzymatic
activity. The structure suggests a model for how interactions with the other
DUBm proteins activate Ubp8 and allows us to speculate about how the DUBm binds
to monoubiquitinated histone H2B in nucleosomes.
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