6GZZ

T. thermophilus hibernating 100S ribosome (amc)

これはPDB形式変換不可エントリーです。

6GZZ の概要

• エントリーDOI: 10.2210/pdb6gzz/pdb
• 関連するPDBエントリー: 6GZQ 6GZX
• EMDBエントリー: 0101 0104 0105
• 分子名称: 50S ribosomal protein L2, 50S ribosomal protein L16, 50S ribosomal protein L17, ... (54 entities in total)
• 機能のキーワード: ribosome, hibernation, 100s, dimer, cryo-em
• 由来する生物種: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579); 詳細
• タンパク質・核酸の鎖数: 108
• 化学式量合計: 4284946.56

構造登録者

Flygaard, R.K.,Jenner, L.B. (登録日: 2018-07-05, 公開日: 2018-10-24, 最終更新日: 2024-05-15)

主引用文献

Flygaard, R.K.,Boegholm, N.,Yusupov, M.,Jenner, L.B.
Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism.
Nat Commun, 9:4179-4179, 2018

PubMed Abstract: In response to cellular stresses bacteria conserve energy by dimerization of ribosomes into inactive hibernating 100S ribosome particles. Ribosome dimerization in Thermus thermophilus is facilitated by hibernation-promoting factor (TtHPF). In this study we demonstrate high sensitivity of Tt100S formation to the levels of TtHPF and show that a 1:1 ratio leads to optimal dimerization. We report structures of the T. thermophilus 100S ribosome determined by cryo-electron microscopy to average resolutions of 4.13 Å and 4.57 Å. In addition, we present a 3.28 Å high-resolution cryo-EM reconstruction of a 70S ribosome from a hibernating ribosome dimer and reveal a role for the linker region connecting the TtHPF N- and C-terminal domains in translation inhibition by preventing Shine-Dalgarno duplex formation. Our work demonstrates that species-specific differences in the dimerization interface govern the overall conformation of the 100S ribosome particle and that for Thermus thermophilus no ribosome-ribosome interactions are involved in the interface.

PubMed: 30301898
DOI: 10.1038/s41467-018-06724-x

実験手法

ELECTRON MICROSCOPY (4.13 Å)