5B33

The crystal structure of the H2AZ nucleosome with H3.3.

5B33 の概要

• エントリーDOI: 10.2210/pdb5b33/pdb
• 関連するPDBエントリー: 5B31 5B32
• 分子名称: Histone H3.3, Histone H4, Histone H2A.Z, ... (5 entities in total)
• 機能のキーワード: histone variant, nucleosome, protein-dna complex, dna binding protein
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Nucleus: P84243 P62805 P0C0S5 P06899
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 200910.82

構造登録者

Horikoshi, N.,Taguchi, H.,Arimura, Y.,Kurumizaka, H. (登録日: 2016-02-08, 公開日: 2016-08-03, 最終更新日: 2023-11-08)

主引用文献

Horikoshi, N.,Arimura, Y.,Taguchi, H.,Kurumizaka, H.
Crystal structures of heterotypic nucleosomes containing histones H2A.Z and H2A.
Open Biology, 6:-, 2016

PubMed Abstract: H2A.Z is incorporated into nucleosomes located around transcription start sites and functions as an epigenetic regulator for the transcription of certain genes. During transcriptional regulation, the heterotypic H2A.Z/H2A nucleosome containing one each of H2A.Z and H2A is formed. However, previous homotypic H2A.Z nucleosome structures suggested that the L1 loop region of H2A.Z would sterically clash with the corresponding region of canonical H2A in the heterotypic nucleosome. To resolve this issue, we determined the crystal structures of heterotypic H2A.Z/H2A nucleosomes. In the H2A.Z/H2A nucleosome structure, the H2A.Z L1 loop structure was drastically altered without any structural changes of the canonical H2A L1 loop, thus avoiding the steric clash. Unexpectedly, the heterotypic H2A.Z/H2A nucleosome is more stable than the homotypic H2A.Z nucleosome. These data suggested that the flexible character of the H2A.Z L1 loop plays an essential role in forming the stable heterotypic H2A.Z/H2A nucleosome.

PubMed: 27358293
DOI: 10.1098/rsob.160127

実験手法

X-RAY DIFFRACTION (2.925 Å)