7Z52

Human NEXT dimer - focused reconstruction of the single MTR4

7Z52 の概要

• エントリーDOI: 10.2210/pdb7z52/pdb
• 関連するPDBエントリー: 7Z4Y
• EMDBエントリー: 14510 14513
• 分子名称: Exosome RNA helicase MTR4, RNA (5'-R(P*UP*UP*UP*UP*U)-3'), Zinc finger CCHC domain-containing protein 8, ... (4 entities in total)
• 機能のキーワード: helicase, atpase, rna degradation, exosome, rna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 199135.51

構造登録者

Gerlach, P.,Lingaraju, M.,Salerno-Kochan, A.,Bonneau, F.,Basquin, J.,Conti, E. (登録日: 2022-03-07, 公開日: 2022-06-22, 最終更新日: 2025-07-09)

主引用文献

Gerlach, P.,Garland, W.,Lingaraju, M.,Salerno-Kochan, A.,Bonneau, F.,Basquin, J.,Jensen, T.H.,Conti, E.
Structure and regulation of the nuclear exosome targeting complex guides RNA substrates to the exosome.
Mol.Cell, 82:2505-, 2022

PubMed Abstract: In mammalian cells, spurious transcription results in a vast repertoire of unproductive non-coding RNAs, whose deleterious accumulation is prevented by rapid decay. The nuclear exosome targeting (NEXT) complex plays a central role in directing non-functional transcripts to exosome-mediated degradation, but the structural and molecular mechanisms remain enigmatic. Here, we elucidated the architecture of the human NEXT complex, showing that it exists as a dimer of MTR4-ZCCHC8-RBM7 heterotrimers. Dimerization preconfigures the major MTR4-binding region of ZCCHC8 and arranges the two MTR4 helicases opposite to each other, with each protomer able to function on many types of RNAs. In the inactive state of the complex, the 3' end of an RNA substrate is enclosed in the MTR4 helicase channel by a ZCCHC8 C-terminal gatekeeping domain. The architecture of a NEXT-exosome assembly points to the molecular and regulatory mechanisms with which the NEXT complex guides RNA substrates to the exosome.

PubMed: 35688157
DOI: 10.1016/j.molcel.2022.04.011

実験手法

ELECTRON MICROSCOPY (3.4 Å)