5HZR

Crystal structure of MtSnf2

5HZR の概要

• エントリーDOI: 10.2210/pdb5hzr/pdb
• 分子名称: SNF2-family ATP dependent chromatin remodeling factor like protein, 3-(1-methylpiperidinium-1-yl)propane-1-sulfonate, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: swi2/snf2, chromatin remodeling, transcription
• 由来する生物種: Myceliophthora thermophila ATCC 42464
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 85748.74

構造登録者

Chen, Z.C.,Xia, X. (登録日: 2016-02-02, 公開日: 2016-07-20, 最終更新日: 2024-03-20)

主引用文献

Xia, X.,Liu, X.,Li, T.,Fang, X.,Chen, Z.C.
Structure of chromatin remodeler Swi2/Snf2 in the resting state
Nat.Struct.Mol.Biol., 23:722-729, 2016

PubMed Abstract: SWI2/SNF2 family proteins regulate a myriad of nucleic acid transactions by sliding, removing and reconstructing nucleosomes in eukaryotic cells. They contain two RecA-like core domains, which couple ATP hydrolysis and DNA translocation to chromatin remodeling. Here we report the crystal structure of Snf2 from the yeast Myceliophthora thermophila. The data show the two RecA-like core domains of Snf2 stacking together and twisting their ATP-binding motifs away from each other, thus explaining the inactivity of the protein in the ground state. We identified several DNA-binding elements, which are fully exposed to solvent, thus suggesting that the protein is poised for its incoming substrate. The catalytic core of Snf2 showed a high chromatin-remodeling activity, which was suppressed by the N-terminal HSA domain. Our findings reveal that the catalytic core of Snf2 is a competent remodeling machine, which rests in an inactive conformation and requires a large conformational change upon activation.

PubMed: 27399259
DOI: 10.1038/nsmb.3259

実験手法

X-RAY DIFFRACTION (2.33 Å)