4ADX

The Cryo-EM Structure of the Archaeal 50S Ribosomal Subunit in Complex with Initiation Factor 6

4ADX の概要

• エントリーDOI: 10.2210/pdb4adx/pdb
• EMDBエントリー: 2012
• 分子名称: 23S ribosomal RNA, 5S Ribosomal RNA, RPL2, ... (36 entities in total)
• 機能のキーワード: ribosome, protein synthesis
• 由来する生物種: METHANOTHERMOBACTER THERMAUTOTROPHICUS; 詳細
• タンパク質・核酸の鎖数: 36
• 化学式量合計: 1551051.09

構造登録者

Greber, B.J.,Boehringer, D.,Godinic-Mikulcic, V.,Crnkovic, A.,Ibba, M.,Weygand-Durasevic, I.,Ban, N. (登録日: 2012-01-04, 公開日: 2012-02-08, 最終更新日: 2024-05-08)

主引用文献

Greber, B.J.,Boehringer, D.,Godinic-Mikulcic, V.,Crnkovic, A.,Ibba, M.,Weygand-Durasevic, I.,Ban, N.
Cryo-Em Structure of the Archaeal 50S Ribosomal Subunit in Complex with Initiation Factor 6 and Implications for Ribosome Evolution
J.Mol.Biol., 418:145-, 2012

PubMed Abstract: Translation of mRNA into proteins by the ribosome is universally conserved in all cellular life. The composition and complexity of the translation machinery differ markedly between the three domains of life. Organisms from the domain Archaea show an intermediate level of complexity, sharing several additional components of the translation machinery with eukaryotes that are absent in bacteria. One of these translation factors is initiation factor 6 (IF6), which associates with the large ribosomal subunit. We have reconstructed the 50S ribosomal subunit from the archaeon Methanothermobacter thermautotrophicus in complex with archaeal IF6 at 6.6 Å resolution using cryo-electron microscopy (EM). The structure provides detailed architectural insights into the 50S ribosomal subunit from a methanogenic archaeon through identification of the rRNA expansion segments and ribosomal proteins that are shared between this archaeal ribosome and eukaryotic ribosomes but are mostly absent in bacteria and in some archaeal lineages. Furthermore, the structure reveals that, in spite of highly divergent evolutionary trajectories of the ribosomal particle and the acquisition of novel functions of IF6 in eukaryotes, the molecular binding of IF6 on the ribosome is conserved between eukaryotes and archaea. The structure also provides a snapshot of the reductive evolution of the archaeal ribosome and offers new insights into the evolution of the translation system in archaea.

PubMed: 22306461
DOI: 10.1016/J.JMB.2012.01.018

実験手法

ELECTRON MICROSCOPY (6.6 Å)