5ND9

Hibernating ribosome from Staphylococcus aureus (Rotated state)

これはPDB形式変換不可エントリーです。

5ND9 の概要

• エントリーDOI: 10.2210/pdb5nd9/pdb
• EMDBエントリー: 3625
• 分子名称: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (52 entities in total)
• 機能のキーワード: s.aureus, hpf, hibernation, 100s ribosome, ribosome
• 由来する生物種: Staphylococcus aureus (strain NCTC 8325); 詳細
• タンパク質・核酸の鎖数: 52
• 化学式量合計: 2165119.28

構造登録者

Khusainov, I.,Vicens, Q.,Ayupov, R.,Usachev, K.,Myasnikov, A.,Simonetti, A.,Validov, S.,Kieffer, B.,Yusupova, G.,Yusupov, M.,Hashem, Y. (登録日: 2017-03-07, 公開日: 2017-06-28, 最終更新日: 2024-05-15)

主引用文献

Khusainov, I.,Vicens, Q.,Ayupov, R.,Usachev, K.,Myasnikov, A.,Simonetti, A.,Validov, S.,Kieffer, B.,Yusupova, G.,Yusupov, M.,Hashem, Y.
Structures and dynamics of hibernating ribosomes from Staphylococcus aureus mediated by intermolecular interactions of HPF.
EMBO J., 36:2073-2087, 2017

PubMed Abstract: In bacteria, ribosomal hibernation shuts down translation as a response to stress, through reversible binding of stress-induced proteins to ribosomes. This process typically involves the formation of 100S ribosome dimers. Here, we present the structures of hibernating ribosomes from human pathogen containing a long variant of the hibernation-promoting factor (SaHPF) that we solved using cryo-electron microscopy. Our reconstructions reveal that the N-terminal domain (NTD) of SaHPF binds to the 30S subunit as observed for shorter variants of HPF in other species. The C-terminal domain (CTD) of SaHPF protrudes out of each ribosome in order to mediate dimerization. Using NMR, we characterized the interactions at the CTD-dimer interface. Secondary interactions are provided by helix 26 of the 16S ribosomal RNA We also show that ribosomes in the 100S particle adopt both rotated and unrotated conformations. Overall, our work illustrates a specific mode of ribosome dimerization by long HPF, a finding that may help improve the selectivity of antimicrobials.

PubMed: 28645916
DOI: 10.15252/embj.201696105

実験手法

ELECTRON MICROSCOPY (3.7 Å)