6NE3

Cryo-EM structure of singly-bound SNF2h-nucleosome complex with SNF2h bound at SHL-2

6NE3 の概要

• エントリーDOI: 10.2210/pdb6ne3/pdb
• EMDBエントリー: 9351 9352 9353 9354 9355 9356
• 分子名称: Histone H3.2, Histone H4, Histone H2A type 1, ... (9 entities in total)
• 機能のキーワード: iswi, chromatin, nucleosome, dna, snf2h, histones, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 254764.68

構造登録者

Armache, J.-P.,Gamarra, N.,Johnson, S.L.,Leonard, J.D.,Wu, S.,Narlikar, G.N.,Cheng, Y. (登録日: 2018-12-16, 公開日: 2019-07-17, 最終更新日: 2024-03-20)

主引用文献

Armache, J.P.,Gamarra, N.,Johnson, S.L.,Leonard, J.D.,Wu, S.,Narlikar, G.J.,Cheng, Y.
Cryo-EM structures of remodeler-nucleosome intermediates suggest allosteric control through the nucleosome.
Elife, 8:-, 2019

PubMed Abstract: The SNF2h remodeler slides nucleosomes most efficiently as a dimer, yet how the two protomers avoid a tug-of-war is unclear. Furthermore, SNF2h couples histone octamer deformation to nucleosome sliding, but the underlying structural basis remains unknown. Here we present cryo-EM structures of SNF2h-nucleosome complexes with ADP-BeF that capture two potential reaction intermediates. In one structure, histone residues near the dyad and in the H2A-H2B acidic patch, distal to the active SNF2h protomer, appear disordered. The disordered acidic patch is expected to inhibit the second SNF2h protomer, while disorder near the dyad is expected to promote DNA translocation. The other structure doesn't show octamer deformation, but surprisingly shows a 2 bp translocation. FRET studies indicate that ADP-BeF predisposes SNF2h-nucleosome complexes for an elemental translocation step. We propose a model for allosteric control through the nucleosome, where one SNF2h protomer promotes asymmetric octamer deformation to inhibit the second protomer, while stimulating directional DNA translocation.

PubMed: 31210637
DOI: 10.7554/eLife.46057

実験手法

ELECTRON MICROSCOPY (3.9 Å)