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PDBsum entry 3wa9
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Structural protein/DNA
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PDB id
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3wa9
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Contents |
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97 a.a.
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78 a.a.
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106 a.a.
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93 a.a.
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84 a.a.
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PDB id:
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| Name: |
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Structural protein/DNA
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Title:
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The nucleosome containing human h2a.Z.1
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Structure:
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Histone h3.1. Chain: a, e. Synonym: histone h3/a, histone h3/b, histone h3/c, histone h3/d, histone h3/f, histone h3/h, histone h3/i, histone h3/j, histone h3/k, histone h3/l. Engineered: yes. Histone h4. Chain: b, f. Engineered: yes.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: h3.1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: h4. Gene: h2a.Z.1. Gene: h2b.
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Resolution:
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3.07Å
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R-factor:
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0.225
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R-free:
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0.271
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Authors:
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N.Horikoshi,K.Sato,K.Shimada,Y.Arimura,A.Osakabe,H.Tachiwana, W.Iwasaki,W.Kagawa,M.Harata,H.Kimura,H.Kurumizaka
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Key ref:
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N.Horikoshi
et al.
(2013).
Structural polymorphism in the L1 loop regions of human H2A.Z.1 and H2A.Z.2.
Acta Crystallogr D Biol Crystallogr,
69,
2431-2439.
PubMed id:
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Date:
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30-Apr-13
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Release date:
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18-Dec-13
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PROCHECK
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Headers
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References
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P68431
(H31_HUMAN) -
Histone H3.1 from Homo sapiens
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Seq:
Struc:
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136 a.a.
97 a.a.
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P62805
(H4_HUMAN) -
Histone H4 from Homo sapiens
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Seq:
Struc:
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103 a.a.
78 a.a.
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P0C0S5
(H2AZ_HUMAN) -
Histone H2A.Z from Homo sapiens
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Seq:
Struc:
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128 a.a.
106 a.a.
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Acta Crystallogr D Biol Crystallogr
69:2431-2439
(2013)
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PubMed id:
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Structural polymorphism in the L1 loop regions of human H2A.Z.1 and H2A.Z.2.
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N.Horikoshi,
K.Sato,
K.Shimada,
Y.Arimura,
A.Osakabe,
H.Tachiwana,
Y.Hayashi-Takanaka,
W.Iwasaki,
W.Kagawa,
M.Harata,
H.Kimura,
H.Kurumizaka.
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ABSTRACT
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The histone H2A.Z variant is widely conserved among eukaryotes. Two isoforms,
H2A.Z.1 and H2A.Z.2, have been identified in vertebrates and may have distinct
functions in cell growth and gene expression. However, no structural differences
between H2A.Z.1 and H2A.Z.2 have been reported. In the present study, the
crystal structures of nucleosomes containing human H2A.Z.1 and H2A.Z.2 were
determined. The structures of the L1 loop regions were found to clearly differ
between H2A.Z.1 and H2A.Z.2, although their amino-acid sequences in this region
are identical. This structural polymorphism may have been induced by a
substitution that evolutionally occurred at the position of amino acid 38 and by
the flexible nature of the L1 loops of H2A.Z.1 and H2A.Z.2. It was also found
that in living cells nucleosomal H2A.Z.1 exchanges more rapidly than H2A.Z.2. A
mutational analysis revealed that the amino-acid difference at position 38 is at
least partially responsible for the distinctive dynamics of H2A.Z.1 and H2A.Z.2.
These findings provide important new information for understanding the
differences in the regulation and functions of H2A.Z.1 and H2A.Z.2 in cells.
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