4CAY

Crystal structure of a human Anp32e-H2A.Z-H2B complex

4CAY の概要

• エントリーDOI: 10.2210/pdb4cay/pdb
• 分子名称: HISTONE H2A.Z, HISTONE H2B TYPE 1-J, ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32 FAMILY MEMBER E, ... (4 entities in total)
• 機能のキーワード: epigenetics, transcription, nucleosome, histone variant, histone chaperone
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Nucleus: P0C0S5 P06899; Cytoplasm : Q9BTT0
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 26396.16

構造登録者

Obri, A.,Ouararhni, K.,Papin, C.,Diebold, M.-L.,Padmanabhan, K.,Marek, M.,Stoll, I.,Roy, L.,Reilly, P.T.,Mak, T.W.,Dimitrov, S.,Romier, C.,Hamiche, A. (登録日: 2013-10-09, 公開日: 2014-01-22, 最終更新日: 2023-12-20)

主引用文献

Obri, A.,Ouararhni, K.,Papin, C.,Diebold, M.-L.,Padmanabhan, K.,Marek, M.,Stoll, I.,Roy, L.,Reilly, P.T.,Wak, T.W.,Dimitrov, S.,Romier, C.,Hamiche, A.
Anp32E is a Histone Chaperone that Removes H2A.Z from Chromatin
Nature, 648:505-, 2014

PubMed Abstract: H2A.Z is an essential histone variant implicated in the regulation of key nuclear events. However, the metazoan chaperones responsible for H2A.Z deposition and its removal from chromatin remain unknown. Here we report the identification and characterization of the human protein ANP32E as a specific H2A.Z chaperone. We show that ANP32E is a member of the presumed H2A.Z histone-exchange complex p400/TIP60. ANP32E interacts with a short region of the docking domain of H2A.Z through a new motif termed H2A.Z interacting domain (ZID). The 1.48 Å resolution crystal structure of the complex formed between the ANP32E-ZID and the H2A.Z/H2B dimer and biochemical data support an underlying molecular mechanism for H2A.Z/H2B eviction from the nucleosome and its stabilization by ANP32E through a specific extension of the H2A.Z carboxy-terminal α-helix. Finally, analysis of H2A.Z localization in ANP32E(-/-) cells by chromatin immunoprecipitation followed by sequencing shows genome-wide enrichment, redistribution and accumulation of H2A.Z at specific chromatin control regions, in particular at enhancers and insulators.

PubMed: 24463511
DOI: 10.1038/NATURE12922

実験手法

X-RAY DIFFRACTION (1.48 Å)