7BTB

Cryo-EM structure of pre-60S ribosome from Saccharomyces cerevisiae rpl4delta63-87 strain at 3.22 Angstroms resolution(state R2)

これはPDB形式変換不可エントリーです。

7BTB の概要

• エントリーDOI: 10.2210/pdb7btb/pdb
• EMDBエントリー: 30174
• 分子名称: 60S ribosomal protein L13-A, 60S ribosomal protein L9-A, 60S ribosomal protein L11-A, ... (56 entities in total)
• 機能のキーワード: pre-60s, rpl4, ribosome
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 53
• 化学式量合計: 2517110.28

構造登録者

Li, Y.,Wilson, D.M. (登録日: 2020-04-01, 公開日: 2020-10-28, 最終更新日: 2024-10-16)

主引用文献

Wilson, D.M.,Li, Y.,LaPeruta, A.,Gamalinda, M.,Gao, N.,Woolford Jr., J.L.
Structural insights into assembly of the ribosomal nascent polypeptide exit tunnel.
Nat Commun, 11:5111-5111, 2020

PubMed Abstract: The nascent polypeptide exit tunnel (NPET) is a major functional center of 60S ribosomal subunits. However, little is known about how the NPET is constructed during ribosome assembly. We utilized molecular genetics, biochemistry, and cryo-electron microscopy (cryo-EM) to investigate the functions of two NPET-associated proteins, ribosomal protein uL4 and assembly factor Nog1, in NPET assembly. Structures of mutant pre-ribosomes lacking the tunnel domain of uL4 reveal a misassembled NPET, including an aberrantly flexible ribosomal RNA helix 74, resulting in at least three different blocks in 60S assembly. Structures of pre-ribosomes lacking the C-terminal extension of Nog1 demonstrate that this extension scaffolds the tunnel domain of uL4 in the NPET to help maintain stability in the core of pre-60S subunits. Our data reveal that uL4 and Nog1 work together in the maturation of ribosomal RNA helix 74, which is required to ensure proper construction of the NPET and 60S ribosomal subunits.

PubMed: 33037216
DOI: 10.1038/s41467-020-18878-8

実験手法

ELECTRON MICROSCOPY (3.22 Å)