5TGC

Structure of the hetero-trimer of Rtt102-Arp7/9 bound to ATP

5TGC の概要

• エントリーDOI: 10.2210/pdb5tgc/pdb
• 分子名称: Actin-related protein 7, Actin-like protein ARP9, Regulator of Ty1 transposition protein 102, ... (5 entities in total)
• 機能のキーワード: chromatin remodeling complexes, actin-related protein, atp-binding site, nuclear actin, structural protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 254243.40

構造登録者

Turegun, B.,Dominguez, R. (登録日: 2016-09-27, 公開日: 2017-09-06, 最終更新日: 2023-10-04)

主引用文献

Turegun, B.,Baker, R.W.,Leschziner, A.E.,Dominguez, R.
Actin-related proteins regulate the RSC chromatin remodeler by weakening intramolecular interactions of the Sth1 ATPase.
Commun Biol, 1:-, 2018

PubMed Abstract: The catalytic subunits of SWI/SNF-family and INO80-family chromatin remodelers bind actin and actin-related proteins (Arps) through an N-terminal helicase/SANT-associated (HSA) domain. Between the HSA and ATPase domains lies a conserved post-HSA (pHSA) domain. The HSA domain of Sth1, the catalytic subunit of the yeast SWI/SNF-family remodeler RSC, recruits the Rtt102-Arp7/9 heterotrimer. Rtt102-Arp7/9 regulates RSC function, but the mechanism is unclear. We show that the pHSA domain interacts directly with another conserved region of the catalytic subunit, protrusion-1. Rtt102-Arp7/9 binding to the HSA domain weakens this interaction and promotes the formation of stable, monodisperse complexes with DNA and nucleosomes. A crystal structure of Rtt102-Arp7/9 shows that ATP binds to Arp7 but not Arp9. However, Arp7 does not hydrolyze ATP. Together, the results suggest that Rtt102 and ATP stabilize a conformation of Arp7/9 that potentiates binding to the HSA domain, which releases intramolecular interactions within Sth1 and controls DNA and nucleosome binding.

PubMed: 29809203
DOI: 10.1038/s42003-017-0002-6

実験手法

X-RAY DIFFRACTION (3.245 Å)