9DUN

Human LAS1L-NOL9 complex

9DUN の概要

• エントリーDOI: 10.2210/pdb9dun/pdb
• EMDBエントリー: 47171
• 分子名称: Polynucleotide 5'-hydroxyl-kinase NOL9, Ribosomal biogenesis protein LAS1L (3 entities in total)
• 機能のキーワード: 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: 6
• 化学式量合計: 198302.04

構造登録者

Huang, J.,Tong, L. (登録日: 2024-10-03, 公開日: 2025-04-30, 最終更新日: 2025-05-28)

主引用文献

Huang, J.,Tong, L.
Molecular insights into the overall architecture of human rixosome.
Nat Commun, 16:3288-3288, 2025

PubMed Abstract: Rixosome is a conserved, multi-subunit protein complex that has critical roles in ribosome biogenesis and silencing of Polycomb target genes. The subunits of human rixosome include PELP1, WDR18, TEX10, LAS1L and NOL9, with LAS1L providing the endoribonuclease activity and NOL9 the RNA 5' kinase activity. We report here cryo-EM structures of the human PELP1-WDR18-TEX10 and LAS1L-NOL9 complexes and a lower-resolution model of the human PELP1-WDR18-LAS1L complex. The structures reveal the overall organization of the human rixosome core scaffold of PELP1-WDR18-TEX10-LAS1L and indicate how the LAS1L-NOL9 endonuclease/kinase catalytic module is recruited to this core scaffold. Each TEX10 molecule has two regions of contact with WDR18, while the helix at the C terminus of WDR18 interacts with the helical domain of LAS1L. The structural observations are supported by our mutagenesis studies. Mutations in both WDR18-TEX10 contact regions can block the binding of TEX10, while truncation of the C-terminal helix of WDR18 can abolish the binding of LAS1L. The structures also reveal substantial conformational differences for TEX10 between the PELP1-WDR18-TEX10 complex alone and that in complex with pre-ribosome.

PubMed: 40195365
DOI: 10.1038/s41467-025-58732-3

実験手法

ELECTRON MICROSCOPY (3.32 Å)