5ME1

Structure of the 30S Pre-Initiation Complex 2 (30S IC-2) Stalled by GE81112

5ME1 の概要

• エントリーDOI: 10.2210/pdb5me1/pdb
• EMDBエントリー: 3495
• 分子名称: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (27 entities in total)
• 機能のキーワード: ribosome, initiation of translation
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 26
• 化学式量合計: 953587.70

構造登録者

Lopez-Alonso, J.P.,Fabbretti, A.,Kaminishi, T.,Iturrioz, I.,Brandi, L.,Gil Carton, D.,Gualerzi, C.,Fucini, P.,Connell, S. (登録日: 2016-11-14, 公開日: 2017-01-11, 最終更新日: 2025-10-01)

主引用文献

Lopez-Alonso, J.P.,Fabbretti, A.,Kaminishi, T.,Iturrioz, I.,Brandi, L.,Gil-Carton, D.,Gualerzi, C.O.,Fucini, P.,Connell, S.R.
Structure of a 30S pre-initiation complex stalled by GE81112 reveals structural parallels in bacterial and eukaryotic protein synthesis initiation pathways.
Nucleic Acids Res., 45:2179-2187, 2017

PubMed Abstract: In bacteria, the start site and the reading frame of the messenger RNA are selected by the small ribosomal subunit (30S) when the start codon, typically an AUG, is decoded in the P-site by the initiator tRNA in a process guided and controlled by three initiation factors. This process can be efficiently inhibited by GE81112, a natural tetrapeptide antibiotic that is highly specific toward bacteria. Here GE81112 was used to stabilize the 30S pre-initiation complex and obtain its structure by cryo-electron microscopy. The results obtained reveal the occurrence of changes in both the ribosome conformation and initiator tRNA position that may play a critical role in controlling translational fidelity. Furthermore, the structure highlights similarities with the early steps of initiation in eukaryotes suggesting that shared structural features guide initiation in all kingdoms of life.

PubMed: 27986852
DOI: 10.1093/nar/gkw1251

実験手法

ELECTRON MICROSCOPY (13.5 Å)