2XQL

Fitting of the H2A-H2B histones in the electron microscopy map of the complex Nucleoplasmin:H2A-H2B histones (1:5).

2XQL の概要

• エントリーDOI: 10.2210/pdb2xql/pdb
• 関連するPDBエントリー: 1EQZ 1HIO 1HQ3 1TZY 2ARO 2HIO
• EMDBエントリー: 1777
• 分子名称: HISTONE H2A-IV, HISTONE H2B 5 (2 entities in total)
• 機能のキーワード: nuclear protein, chaperone, chromatin, nuclear-chaperone, histone-chaperone
• 由来する生物種: GALLUS GALLUS (CHICKEN); 詳細
• 細胞内の位置: Nucleus: P02263 P0C1H4
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 100060.40

構造登録者

Ramos, I.,Martin-Benito, J.,Finn, R.,Bretana, L.,Aloria, K.,Arizmendi, J.M.,Ausio, J.,Muga, A.,Valpuesta, J.M.,Prado, A. (登録日: 2010-09-02, 公開日: 2010-11-03, 最終更新日: 2024-05-08)

主引用文献

Ramos, I.,Martin-Benito, J.,Finn, R.,Bretana, L.,Aloria, K.,Arizmendi, J.M.,Ausio, J.,Muga, A.,Valpuesta, J.M.,Prado, A.
Nucleoplasmin Binds Histone H2A-H2B Dimers Through its Distal Face.
J.Biol.Chem., 285:33771-, 2010

PubMed Abstract: Nucleoplasmin (NP) is a pentameric chaperone that regulates the condensation state of chromatin extracting specific basic proteins from sperm chromatin and depositing H2A-H2B histone dimers. It has been proposed that histones could bind to either the lateral or distal face of the pentameric structure. Here, we combine different biochemical and biophysical techniques to show that natural, hyperphosphorylated NP can bind five H2A-H2B dimers and that the amount of bound ligand depends on the overall charge (phosphorylation level) of the chaperone. Three-dimensional reconstruction of NP/H2A-H2B complex carried out by electron microscopy reveals that histones interact with the chaperone distal face. Limited proteolysis and mass spectrometry indicate that the interaction results in protection of the histone fold and most of the H2A and H2B C-terminal tails. This structural information can help to understand the function of NP as a histone chaperone.

PubMed: 20696766
DOI: 10.1074/JBC.M110.150664

実験手法

ELECTRON MICROSCOPY (19.5 Å)