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4KUL

Crystal structure of N-terminal acetylated yeast Sir3 BAH domain V83P mutant

4KUL の概要
エントリーDOI10.2210/pdb4kul/pdb
関連するPDBエントリー4KUD 4KUI
分子名称Regulatory protein SIR3 (2 entities in total)
機能のキーワードbah domain, silencing, nucleus, transcription
由来する生物種Saccharomyces cerevisiae (yeast)
細胞内の位置Nucleus: P06701
タンパク質・核酸の鎖数1
化学式量合計26772.28
構造登録者
Yang, D.,Fang, Q.,Wang, M.,Ren, R.,Wang, H.,He, M.,Sun, Y.,Yang, N.,Xu, R.M. (登録日: 2013-05-22, 公開日: 2013-08-07, 最終更新日: 2023-11-08)
主引用文献Yang, D.,Fang, Q.,Wang, M.,Ren, R.,Wang, H.,He, M.,Sun, Y.,Yang, N.,Xu, R.M.
N alpha-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain.
Nat.Struct.Mol.Biol., 20:1116-1118, 2013
Cited by
PubMed Abstract: In Saccharomyces cerevisiae, acetylation of the Sir3 N terminus is important for transcriptional silencing. This covalent modification promotes the binding of the Sir3 BAH domain to the nucleosome, but a mechanistic understanding of this phenomenon is lacking. By X-ray crystallography, we show here that the acetylated N terminus of Sir3 does not interact with the nucleosome directly. Instead, it stabilizes a nucleosome-binding loop in the BAH domain.
PubMed: 23934152
DOI: 10.1038/nsmb.2637
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.62 Å)
構造検証レポート
Validation report summary of 4kul
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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