6HTS

Cryo-EM structure of the human INO80 complex bound to nucleosome

「6ETX」から置き換えられました

6HTS の概要

• エントリーDOI: 10.2210/pdb6hts/pdb
• EMDBエントリー: 3954
• 分子名称: RuvB-like 1, DNA (150-MER), ADENOSINE-5'-DIPHOSPHATE, ... (13 entities in total)
• 機能のキーワード: chromatin, remodeller, nucleosome, dna binding, histones, dna repair, atpase, helicase, sliding, complex, dna binding protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 19
• 化学式量合計: 811323.31

構造登録者

Ayala, R.,Willhoft, O.,Aramayo, R.J.,Wilkinson, M.,McCormack, E.A.,Ocloo, L.,Wigley, D.B.,Zhang, X. (登録日: 2018-10-04, 公開日: 2018-11-07, 最終更新日: 2025-07-09)

主引用文献

Ayala, R.,Willhoft, O.,Aramayo, R.J.,Wilkinson, M.,McCormack, E.A.,Ocloo, L.,Wigley, D.B.,Zhang, X.
Structure and regulation of the human INO80-nucleosome complex.
Nature, 556:391-395, 2018

PubMed Abstract: Access to DNA within nucleosomes is required for a variety of processes in cells including transcription, replication and repair. Consequently, cells encode multiple systems that remodel nucleosomes. These complexes can be simple, involving one or a few protein subunits, or more complicated multi-subunit machines . Biochemical studies have placed the motor domains of several chromatin remodellers in the superhelical location 2 region of the nucleosome. Structural studies of yeast Chd1 and Snf2-a subunit in the complex with the capacity to remodel the structure of chromatin (RSC)-in complex with nucleosomes have provided insights into the basic mechanism of nucleosome sliding performed by these complexes. However, how larger, multi-subunit remodelling complexes such as INO80 interact with nucleosomes and how remodellers carry out functions such as nucleosome sliding , histone exchange and nucleosome spacing remain poorly understood. Although some remodellers work as monomers , others work as highly cooperative dimers. Here we present the structure of the human INO80 chromatin remodeller with a bound nucleosome, which reveals that INO80 interacts with nucleosomes in a previously undescribed manner: the motor domains are located on the DNA at the entry point to the nucleosome, rather than at superhelical location 2. The ARP5-IES6 module of INO80 makes additional contacts on the opposite side of the nucleosome. This arrangement enables the histone H3 tails of the nucleosome to have a role in the regulation of the activities of the INO80 motor domain-unlike in other characterized remodellers, for which H4 tails have been shown to regulate the motor domains.

PubMed: 29643506
DOI: 10.1038/s41586-018-0021-6

実験手法

ELECTRON MICROSCOPY (4.8 Å)