 |
PDBsum entry 4zux
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Hydrolase/DNA
|
PDB id
|
|
|
|
4zux
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
97 a.a.
|
|
|
|
|
|
|
|
|
|
|
83 a.a.
|
|
|
|
|
|
|
|
|
|
|
103 a.a.
|
|
|
|
|
|
|
|
|
|
|
95 a.a.
|
|
|
|
|
|
|
|
|
|
|
78 a.a.
|
|
|
|
|
|
|
|
|
|
|
447 a.a.
|
|
|
|
|
|
|
|
|
|
|
89 a.a.
|
|
|
|
|
|
|
|
|
|
|
90 a.a.
|
|
|
|
|
|
|
|
|
|
|
76 a.a.
|
|
|
|
|
|
|
|
|
|
|
82 a.a.
|
|
|
|
|
|
|
|
|
|
|
90 a.a.
|
|
|
|
|
|
|
|
|
|
|
89 a.a.
|
|
|
|
|
|
|
|
|
|
|
85 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structural basis for histone h2b deubiquitination by the saga dub module.
|
|
|
Authors
|
|
M.T.Morgan,
M.Haj-Yahya,
A.E.Ringel,
P.Bandi,
A.Brik,
C.Wolberger.
|
|
|
Ref.
|
|
Science, 2016,
351,
725-728.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Monoubiquitinated histone H2B plays multiple roles in transcription activation.
H2B is deubiquitinated by the Spt-Ada-Gcn5 acetyltransferase (SAGA) coactivator,
which contains a four-protein subcomplex known as the deubiquitinating (DUB)
module. The crystal structure of the Ubp8/Sgf11/Sus1/Sgf73 DUB module bound to a
ubiquitinated nucleosome reveals that the DUB module primarily contacts H2A/H2B,
with an arginine cluster on the Sgf11 zinc finger domain docking on the
conserved H2A/H2B acidic patch. The Ubp8 catalytic domain mediates additional
contacts with H2B, as well as with the conjugated ubiquitin. We find that the
DUB module deubiquitinates H2B both in the context of the nucleosome and in
H2A/H2B dimers complexed with the histone chaperone, FACT, suggesting that SAGA
could target H2B at multiple stages of nucleosome disassembly and reassembly
during transcription.
|
|
|
|
|
|
|
