6O22

Structure of Asf1-H3:H4-Rtt109-Vps75 histone chaperone-lysine acetyltransferase complex with the histone substrate.

6O22 の概要

• エントリーDOI: 10.2210/pdb6o22/pdb
• NMR情報: BMRB: 30576
• 分子名称: Vacuolar protein sorting-associated protein 75, Histone acetyltransferase RTT109, Histone chaperone ASF1, ... (5 entities in total)
• 機能のキーワード: chaperone
• 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: 6
• 化学式量合計: 170478.27

構造登録者

Danilenko, N.,Carlomagno, T.,Kirkpatrick, J.P. (登録日: 2019-02-22, 公開日: 2019-07-31, 最終更新日: 2024-05-01)

主引用文献

Danilenko, N.,Lercher, L.,Kirkpatrick, J.,Gabel, F.,Codutti, L.,Carlomagno, T.
Histone chaperone exploits intrinsic disorder to switch acetylation specificity.
Nat Commun, 10:3435-3435, 2019

PubMed Abstract: Histones, the principal protein components of chromatin, contain long disordered sequences, which are extensively post-translationally modified. Although histone chaperones are known to control both the activity and specificity of histone-modifying enzymes, the mechanisms promoting modification of highly disordered substrates, such as lysine-acetylation within the N-terminal tail of histone H3, are not understood. Here, to understand how histone chaperones Asf1 and Vps75 together promote H3 K9-acetylation, we establish the solution structural model of the acetyltransferase Rtt109 in complex with Asf1 and Vps75 and the histone dimer H3:H4. We show that Vps75 promotes K9-acetylation by engaging the H3 N-terminal tail in fuzzy electrostatic interactions with its disordered C-terminal domain, thereby confining the H3 tail to a wide central cavity faced by the Rtt109 active site. These fuzzy interactions between disordered domains achieve localization of lysine residues in the H3 tail to the catalytic site with minimal loss of entropy, and may represent a common mechanism of enzymatic reactions involving highly disordered substrates.

PubMed: 31387991
DOI: 10.1038/s41467-019-11410-7

実験手法

SOLUTION NMR
SOLUTION SCATTERING