 |
PDBsum entry 3w96
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Structural protein/DNA
|
PDB id
|
|
|
|
3w96
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
96 a.a.
|
|
|
|
|
|
|
|
|
|
|
77 a.a.
|
|
|
|
|
|
|
|
|
|
|
107 a.a.
|
|
|
|
|
|
|
|
|
|
|
95 a.a.
|
|
|
|
|
|
|
|
|
|
|
82 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Contribution of histone n-Terminal tails to the structure and stability of nucleosomes.
|
|
|
Authors
|
|
W.Iwasaki,
Y.Miya,
N.Horikoshi,
A.Osakabe,
H.Taguchi,
H.Tachiwana,
T.Shibata,
W.Kagawa,
H.Kurumizaka.
|
|
|
Ref.
|
|
Febs Open Bio, 2013,
3,
363-369.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
|
|
|
|
Abstract
|
|
|
Histones are the protein components of the nucleosome, which forms the basic
architecture of eukaryotic chromatin. Histones H2A, H2B, H3, and H4 are composed
of two common regions, the "histone fold" and the "histone
tail". Many efforts have been focused on the mechanisms by which the
post-translational modifications of histone tails regulate the higher-order
chromatin architecture. On the other hand, previous biochemical studies have
suggested that histone tails also affect the structure and stability of the
nucleosome core particle itself. However, the precise contributions of each
histone tail are unclear. In the present study, we determined the crystal
structures of four mutant nucleosomes, in which one of the four histones, H2A,
H2B, H3, or H4, lacked the N-terminal tail. We found that the deletion of the
H2B or H3 N-terminal tail affected histone-DNA interactions and substantially
decreased nucleosome stability. These findings provide important information for
understanding the complex roles of histone tails in regulating chromatin
structure.
|
|
|
|
|
|
|
