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8IFG

Cryo-EM structure of the Clr6S (Clr6-HDAC) complex from S. pombe

8IFG の概要
エントリーDOI10.2210/pdb8ifg/pdb
EMDBエントリー35416 35417 36278
分子名称RbAp48-related WD40 repeat-containing protein prw1, Paired amphipathic helix protein pst2, Histone deacetylase clr6, ... (8 entities in total)
機能のキーワードrpd3s, histone deacetylase, hdac, clr6, rpd3, clr6s, clr6 hdac, transcription
由来する生物種Schizosaccharomyces pombe (strain 972 / ATCC 24843)
詳細
タンパク質・核酸の鎖数7
化学式量合計411810.32
構造登録者
Zhang, H.Q.,Wang, X.,Wang, Y.N.,Liu, S.M.,Zhang, Y.,Xu, K.,Ji, L.T.,Kornberg, R.D. (登録日: 2023-02-17, 公開日: 2024-01-03, 最終更新日: 2025-07-23)
主引用文献Wang, X.,Wang, Y.,Liu, S.,Zhang, Y.,Xu, K.,Ji, L.,Kornberg, R.D.,Zhang, H.
Class I histone deacetylase complex: Structure and functional correlates.
Proc Natl Acad Sci U S A, 120:e2307598120-, 2023
Cited by
PubMed Abstract: The Clr6S complex, a class I histone deacetylase complex, functions as a zinc-dependent enzyme to remove acetyl groups from lysine residues in histone tails. We report here the cryo-EM structure of Clr6S alone and a cryo-EM map of Clr6S in complex with a nucleosome. The active center, revealed at near-atomic resolution, includes features important for catalysis-A water molecule coordinated by zinc, the likely nucleophile for attack on the acetyl-lysine bond, and a loop that may position the substrate for catalysis. The cryo-EM map in the presence of a nucleosome reveals multiple Clr6S-nucleosome contacts and a high degree of relative motion of Clr6S and the nucleosome. Such flexibility may be attributed to interaction at a site in the flexible histone tail and is likely important for the function of the deacetylase, which acts at multiple sites in other histone tails.
PubMed: 37459529
DOI: 10.1073/pnas.2307598120
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.2 Å)
構造検証レポート
Validation report summary of 8ifg
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2026-04-22に公開中

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