5ZET

M. smegmatis P/P state 50S ribosomal subunit

5ZET の概要

• エントリーDOI: 10.2210/pdb5zet/pdb
• EMDBエントリー: 6922
• 分子名称: 50S ribosomal protein L2, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (34 entities in total)
• 機能のキーワード: translating-state, ribosome, complex
• 由来する生物種: Mycobacterium smegmatis str. MC2 155; 詳細
• タンパク質・核酸の鎖数: 34
• 化学式量合計: 1485560.76

構造登録者

Mishra, S.,Ahmed, T.,Tyagi, A.,Shi, J.,Bhushan, S. (登録日: 2018-02-28, 公開日: 2018-09-26)

主引用文献

Mishra, S.,Ahmed, T.,Tyagi, A.,Shi, J.,Bhushan, S.
Structures of Mycobacterium smegmatis 70S ribosomes in complex with HPF, tmRNA, and P-tRNA.
Sci Rep, 8:13587-13587, 2018

PubMed Abstract: Ribosomes are the dynamic protein synthesis machineries of the cell. They may exist in different functional states in the cell. Therefore, it is essential to have structural information on these different functional states of ribosomes to understand their mechanism of action. Here, we present single particle cryo-EM reconstructions of the Mycobacterium smegmatis 70S ribosomes in the hibernating state (with HPF), trans-translating state (with tmRNA), and the P/P state (with P-tRNA) resolved to 4.1, 12.5, and 3.4 Å, respectively. A comparison of the P/P state with the hibernating state provides possible functional insights about the Mycobacteria-specific helix H54a rRNA segment. Interestingly, densities for all the four OB domains of bS1 protein is visible in the hibernating 70S ribosome displaying the molecular details of bS1-70S interactions. Our structural data shows a Mycobacteria-specific H54a-bS1 interaction which seems to prevent subunit dissociation and degradation during hibernation without the formation of 100S dimer. This indicates a new role of bS1 protein in 70S protection during hibernation in Mycobacteria in addition to its conserved function during translation initiation.

PubMed: 30206241
DOI: 10.1038/s41598-018-31850-3

実験手法

ELECTRON MICROSCOPY (3.2 Å)