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PDBsum entry 5b0z
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DNA binding protein
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PDB id
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5b0z
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Contents |
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96 a.a.
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78 a.a.
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108 a.a.
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94 a.a.
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83 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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Crystal structure of the nucleosome containing histone h3 with crotonylated lysine 122.
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Authors
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Y.Suzuki,
N.Horikoshi,
D.Kato,
H.Kurumizaka.
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Ref.
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Biochem Biophys Res Commun, 2016,
469,
483-489.
[DOI no: ]
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PubMed id
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Abstract
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The crotonylation of histones is an important post-translational modification,
and epigenetically functions in the regulation of genomic DNA activity. The
histone modifications in the structured "histone-fold" domains are
considered to have an especially important impact on the nucleosome structure
and dynamics. In the present study, we reconstituted the human nucleosome
containing histone H3.2 crotonylated at the Lys122 residue, and determined its
crystal structure at 2.56 Å resolution. We found that the crotonylation of the
H3 Lys122 residue does not affect the overall nucleosome structure, but locally
impedes the formation of the water-mediated hydrogen bond with the DNA backbone.
Consistently, thermal stability assays revealed that the H3 Lys122
crotonylation, as well as the H3 Lys122 acetylation, clearly reduced the
histone-DNA association.
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