6RO1

X-ray crystal structure of the MTR4 NVL complex

6RO1 の概要

• エントリーDOI: 10.2210/pdb6ro1/pdb
• 分子名称: Exosome RNA helicase MTR4, Nuclear valosin-containing protein-like, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: dexh helicase, complex, 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: 2
• 化学式量合計: 117653.42

構造登録者

Lingaraju, M.,Langer, L.M.,Basquin, J.,Falk, S.,Conti, E. (登録日: 2019-05-10, 公開日: 2019-07-03, 最終更新日: 2024-01-24)

主引用文献

Lingaraju, M.,Johnsen, D.,Schlundt, A.,Langer, L.M.,Basquin, J.,Sattler, M.,Heick Jensen, T.,Falk, S.,Conti, E.
The MTR4 helicase recruits nuclear adaptors of the human RNA exosome using distinct arch-interacting motifs.
Nat Commun, 10:3393-3393, 2019

PubMed Abstract: The nuclear exosome and its essential co-factor, the RNA helicase MTR4, play crucial roles in several RNA degradation pathways. Besides unwinding RNA substrates for exosome-mediated degradation, MTR4 associates with RNA-binding proteins that function as adaptors in different RNA processing and decay pathways. Here, we identify and characterize the interactions of human MTR4 with a ribosome processing adaptor, NVL, and with ZCCHC8, an adaptor involved in the decay of small nuclear RNAs. We show that the unstructured regions of NVL and ZCCHC8 contain short linear motifs that bind the MTR4 arch domain in a mutually exclusive manner. These short sequences diverged from the arch-interacting motif (AIM) of yeast rRNA processing factors. Our results suggest that nuclear exosome adaptors have evolved canonical and non-canonical AIM sequences to target human MTR4 and demonstrate the versatility and specificity with which the MTR4 arch domain can recruit a repertoire of different RNA-binding proteins.

PubMed: 31358741
DOI: 10.1038/s41467-019-11339-x

実験手法

X-RAY DIFFRACTION (3.07 Å)