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6ISO

Human SIRT3 Recognizing H3K4cr

4V1C」から置き換えられました
6ISO の概要
エントリーDOI10.2210/pdb6iso/pdb
分子名称NAD-dependent protein deacetylase sirtuin-3, mitochondrial, ARG-THR-LYS-GLN-THR-ALA-ARG, ZINC ION, ... (6 entities in total)
機能のキーワードposttranslational modification, sirtuins, histones, complex., hydrolase
由来する生物種Homo sapiens (Human)
詳細
タンパク質・核酸の鎖数12
化学式量合計189691.77
構造登録者
Wang, Y.,Hao, Q. (登録日: 2018-11-17, 公開日: 2019-01-23, 最終更新日: 2024-11-20)
主引用文献Bao, X.,Wang, Y.,Li, X.,Li, X.M.,Liu, Z.,Yang, T.,Wong, C.F.,Zhang, J.,Hao, Q.,Li, X.D.
Identification of 'erasers' for lysine crotonylated histone marks using a chemical proteomics approach.
Elife, 3:-, 2014
Cited by
PubMed Abstract: Posttranslational modifications (PTMs) play a crucial role in a wide range of biological processes. Lysine crotonylation (Kcr) is a newly discovered histone PTM that is enriched at active gene promoters and potential enhancers in mammalian cell genomes. However, the cellular enzymes that regulate the addition and removal of Kcr are unknown, which has hindered further investigation of its cellular functions. Here we used a chemical proteomics approach to comprehensively profile 'eraser' enzymes that recognize a lysine-4 crotonylated histone H3 (H3K4Cr) mark. We found that Sirt1, Sirt2, and Sirt3 can catalyze the hydrolysis of lysine crotonylated histone peptides and proteins. More importantly, Sirt3 functions as a decrotonylase to regulate histone Kcr dynamics and gene transcription in living cells. This discovery not only opens opportunities for examining the physiological significance of histone Kcr, but also helps to unravel the unknown cellular mechanisms controlled by Sirt3, that have previously been considered solely as a deacetylase.
PubMed: 25369635
DOI: 10.7554/eLife.02999
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.95 Å)
構造検証レポート
Validation report summary of 6iso
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2025-12-31に公開中

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