8GA8

Structure of the yeast (HDAC) Rpd3L complex

8GA8 の概要

• エントリーDOI: 10.2210/pdb8ga8/pdb
• EMDBエントリー: 29892
• 分子名称: Transcriptional regulatory protein SDS3, Transcriptional regulatory protein SIN3, Transcriptional regulatory protein SAP30, ... (9 entities in total)
• 機能のキーワード: hdac, silencing, chromatin, transcription
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 675551.55

構造登録者

Patel, A.B.,Radhakrishnan, I.,He, Y. (登録日: 2023-02-22, 公開日: 2023-07-12, 最終更新日: 2024-06-19)

主引用文献

Patel, A.B.,Qing, J.,Tam, K.H.,Zaman, S.,Luiso, M.,Radhakrishnan, I.,He, Y.
Cryo-EM structure of the Saccharomyces cerevisiae Rpd3L histone deacetylase complex.
Nat Commun, 14:3061-3061, 2023

PubMed Abstract: The Rpd3L histone deacetylase (HDAC) complex is an ancient 12-subunit complex conserved in a broad range of eukaryotes that performs localized deacetylation at or near sites of recruitment by DNA-bound factors. Here we describe the cryo-EM structure of this prototypical HDAC complex that is characterized by as many as seven subunits performing scaffolding roles for the tight integration of the only catalytic subunit, Rpd3. The principal scaffolding protein, Sin3, along with Rpd3 and the histone chaperone, Ume1, are present in two copies, with each copy organized into separate lobes of an asymmetric dimeric molecular assembly. The active site of one Rpd3 is completely occluded by a leucine side chain of Rxt2, while the tips of the two lobes and the more peripherally associated subunits exhibit varying levels of flexibility and positional disorder. The structure reveals unexpected structural homology/analogy between unrelated subunits in the fungal and mammalian complexes and provides a foundation for deeper interrogations of structure, biology, and mechanism of these complexes, as well as for the discovery of HDAC complex-specific inhibitors.

PubMed: 37244892
DOI: 10.1038/s41467-023-38687-z

実験手法

ELECTRON MICROSCOPY (3.5 Å)