1YD9

1.6A Crystal Structure of the Non-Histone Domain of the Histone Variant MacroH2A1.1.

1YD9 の概要

• エントリーDOI: 10.2210/pdb1yd9/pdb
• 関連するPDBエントリー: 1BFR 1HJZ 1VHU
• 分子名称: Core histone macro-H2A.1, GOLD ION (3 entities in total)
• 機能のキーワード: alpha-beta structure, a1pp domain, macro-domain, structural protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Nucleus (By similarity): Q02874
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 82941.95

構造登録者

Chakravarthy, S.,Swamy, G.Y.S.K.,Caron, C.,Perche, P.Y.,Pehrson, J.R.,Khochbin, S.,Luger, K. (登録日: 2004-12-23, 公開日: 2005-09-27, 最終更新日: 2024-02-14)

主引用文献

Chakravarthy, S.,Gundimella, S.K.,Caron, C.,Perche, P.Y.,Pehrson, J.R.,Khochbin, S.,Luger, K.
Structural characterization of the histone variant macroH2A
Mol.Cell.Biol., 25:7616-7624, 2005

PubMed Abstract: macroH2A is an H2A variant with a highly unusual structural organization. It has a C-terminal domain connected to the N-terminal histone domain by a linker. Crystallographic and biochemical studies show that changes in the L1 loop in the histone fold region of macroH2A impact the structure and potentially the function of nucleosomes. The 1.6-A X-ray structure of the nonhistone region reveals an alpha/beta fold which has previously been found in a functionally diverse group of proteins. This region associates with histone deacetylases and affects the acetylation status of nucleosomes containing macroH2A. Thus, the unusual domain structure of macroH2A integrates independent functions that are instrumental in establishing a structurally and functionally unique chromatin domain.

PubMed: 16107708
DOI: 10.1128/MCB.25.17.7616-7624.2005

実験手法

X-RAY DIFFRACTION (1.6 Å)