5NBN

Crystal structure of the Arp4-N-actin-Arp8-Ino80HSA module of INO80

5NBN の概要

• エントリーDOI: 10.2210/pdb5nbn/pdb
• 関連するPDBエントリー: 5NBL 5NBM
• 分子名称: Actin-related protein 4, Actin, Actin-like protein ARP8, ... (7 entities in total)
• 機能のキーワード: chromatin remodeling, nanobody, ino80, swr1, nua4, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 376334.93

構造登録者

Knoll, K.R.,Eustermann, S.,Hopfner, K.P. (登録日: 2017-03-02, 公開日: 2018-08-22, 最終更新日: 2024-01-17)

主引用文献

Knoll, K.R.,Eustermann, S.,Niebauer, V.,Oberbeckmann, E.,Stoehr, G.,Schall, K.,Tosi, A.,Schwarz, M.,Buchfellner, A.,Korber, P.,Hopfner, K.P.
The nuclear actin-containing Arp8 module is a linker DNA sensor driving INO80 chromatin remodeling.
Nat. Struct. Mol. Biol., 25:823-832, 2018

PubMed Abstract: Nuclear actin (N-actin) and actin-related proteins (Arps) are critical components of several chromatin modulating complexes, including the chromatin remodeler INO80, but their function is largely elusive. Here, we report the crystal structure of the 180-kDa Arp8 module of Saccharomyces cerevisiae INO80 and establish its role in recognition of extranucleosomal linker DNA. Arp8 engages N-actin in a manner distinct from that of other actin-fold proteins and thereby specifies recruitment of the Arp4-N-actin heterodimer to a segmented scaffold of the helicase-SANT-associated (HSA) domain of Ino80. The helical HSA domain spans over 120 Å and provides an extended binding platform for extranucleosomal entry DNA that is required for nucleosome sliding and genome-wide nucleosome positioning. Together with the recent cryo-electron microscopy structure of INO80-nucleosome complex, our findings suggest an allosteric mechanism by which INO80 senses 40-bp linker DNA to conduct highly processive chromatin remodeling.

PubMed: 30177756
DOI: 10.1038/s41594-018-0115-8

実験手法

X-RAY DIFFRACTION (4 Å)