5FUG

Crystal structure of a human YL1-H2A.Z-H2B complex

5FUG の概要

• エントリーDOI: 10.2210/pdb5fug/pdb
• 関連するPDBエントリー: 5FUE
• 分子名称: HISTONE H2A.Z, HISTONE H2B TYPE 1-J, VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 72 HOMOLOG, ... (4 entities in total)
• 機能のキーワード: dna binding protein, histone, chaperone, remodeler, h2a.z, yl1
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Nucleus: P0C0S5 P06899 Q15906
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 120746.96

構造登録者

Latrick, C.M.,Marek, M.,Ouararhni, K.,Papin, C.,Stoll, I.,Ignatyeva, M.,Obri, A.,Ennifar, E.,Dimitrov, S.,Romier, C.,Hamiche, A. (登録日: 2016-01-27, 公開日: 2016-03-09, 最終更新日: 2024-01-10)

主引用文献

Latrick, C.M.,Marek, M.,Ouararhni, K.,Papin, C.,Stoll, I.,Ignatyeva, M.,Obri, A.,Ennifar, E.,Dimitrov, S.,Romier, C.,Hamiche, A.
Molecular Basis and Specificity of H2A.Z-H2B Recognition and Deposition by the Histone Chaperone Yl1
Nat.Struct.Mol.Biol., 23:309-, 2016

PubMed Abstract: H2A.Z, a widely conserved histone variant, is evicted from chromatin by the histone chaperone ANP32E. However, to date, no deposition chaperone for H2A.Z is known in metazoans. Here, we identify YL1 as a specific H2A.Z-deposition chaperone. The 2.7-Å-resolution crystal structure of the human YL1-H2A.Z-H2B complex shows that YL1 binding, similarly to ANP32E binding, triggers an extension of the H2A.Z αC helix. The interaction with YL1 is, however, more extensive and includes both the extended acidic patch and the entire DNA-binding surface of H2A.Z-H2B. Substitution of only four amino acid residues of H2A is sufficient for the formation of an H2A.Z-like interface specifically recognized by YL1. Collectively, our data reveal the molecular basis of H2A.Z-specific recognition by YL1 and shed light on the mechanism of H2A.Z transfer to the nucleosome by the ATP-dependent chromatin-remodeling complexes SRCAP and P400-TIP60.

PubMed: 26974126
DOI: 10.1038/NSMB.3189

実験手法

X-RAY DIFFRACTION (2.7 Å)