4FO0

Human actin-related protein Arp8 in its ATP-bound state

4FO0 の概要

• エントリーDOI: 10.2210/pdb4fo0/pdb
• 関連するPDBエントリー: 3QB0
• 分子名称: Actin-related protein 8, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: actin-related protein, chromatin remodeling, nucleosomes, nucleus, gene regulation
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus : Q9H981
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 68424.40

構造登録者

Gerhold, C.B.,Lakomek, K.,Seifert, F.U.,Hopfner, K.-P. (登録日: 2012-06-20, 公開日: 2012-09-26, 最終更新日: 2023-09-13)

主引用文献

Gerhold, C.B.,Winkler, D.D.,Lakomek, K.,Seifert, F.U.,Fenn, S.,Kessler, B.,Witte, G.,Luger, K.,Hopfner, K.P.
Structure of Actin-related protein 8 and its contribution to nucleosome binding.
Nucleic Acids Res., 40:11036-11046, 2012

PubMed Abstract: Nuclear actin-related proteins (Arps) are subunits of several chromatin remodelers, but their molecular functions within these complexes are unclear. We report the crystal structure of the INO80 complex subunit Arp8 in its ATP-bound form. Human Arp8 has several insertions in the conserved actin fold that explain its inability to polymerize. Most remarkably, one insertion wraps over the active site cleft and appears to rigidify the domain architecture, while active site features shared with actin suggest an allosterically controlled ATPase activity. Quantitative binding studies with nucleosomes and histone complexes reveal that Arp8 and the Arp8-Arp4-actin-HSA sub-complex of INO80 strongly prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting that Arp8 functions as a nucleosome recognition module. In contrast, Arp4 prefers free (H3-H4)(2) over nucleosomes and may serve remodelers through binding to (dis)assembly intermediates in the remodeling reaction.

PubMed: 22977180
DOI: 10.1093/nar/gks842

実験手法

X-RAY DIFFRACTION (2.6 Å)