4V6U

Promiscuous behavior of proteins in archaeal ribosomes revealed by cryo-EM: implications for evolution of eukaryotic ribosomes

これはPDB形式変換不可エントリーです。

4V6U の概要

• エントリーDOI: 10.2210/pdb4v6u/pdb
• EMDBエントリー: 2009
• 分子名称: 30S ribosomal protein S15P/S13e, 30S ribosomal protein S4P, E-tRNA, ... (68 entities in total)
• 機能のキーワード: archaea, archaeal, ribosomal, 70s, kink-turn, protein synthesis, rna, ribosome
• 由来する生物種: Pyrococcus furiosus; 詳細
• タンパク質・核酸の鎖数: 72
• 化学式量合計: 2602985.23

構造登録者

Armache, J.-P.,Anger, A.M.,Marquez, V.,Frankenberg, S.,Froehlich, T.,Villa, E.,Berninghausen, O.,Thomm, M.,Arnold, G.J.,Beckmann, R.,Wilson, D.N. (登録日: 2012-08-09, 公開日: 2014-07-09, 最終更新日: 2024-05-15)

主引用文献

Armache, J.-P.,Anger, A.M.,Marquez, V.,Franckenberg, S.,Frohlich, T.,Villa, E.,Berninghausen, O.,Thomm, M.,Arnold, G.J.,Beckmann, R.,Wilson, D.N.
Promiscuous behaviour of archaeal ribosomal proteins: Implications for eukaryotic ribosome evolution.
Nucleic Acids Res., 41:1284-1293, 2013

PubMed Abstract: In all living cells, protein synthesis occurs on ribonucleoprotein particles called ribosomes. Molecular models have been reported for complete bacterial 70S and eukaryotic 80S ribosomes; however, only molecular models of large 50S subunits have been reported for archaea. Here, we present a complete molecular model for the Pyrococcus furiosus 70S ribosome based on a 6.6 Å cryo-electron microscopy map. Moreover, we have determined cryo-electron microscopy reconstructions of the Euryarchaeota Methanococcus igneus and Thermococcus kodakaraensis 70S ribosomes and Crenarchaeota Staphylothermus marinus 50S subunit. Examination of these structures reveals a surprising promiscuous behavior of archaeal ribosomal proteins: We observe intersubunit promiscuity of S24e and L8e (L7ae), the latter binding to the head of the small subunit, analogous to S12e in eukaryotes. Moreover, L8e and L14e exhibit intrasubunit promiscuity, being present in two copies per archaeal 50S subunit, with the additional binding site of L14e analogous to the related eukaryotic r-protein L27e. Collectively, these findings suggest insights into the evolution of eukaryotic ribosomal proteins through increased copy number and binding site promiscuity.

PubMed: 23222135
DOI: 10.1093/nar/gks1259

実験手法

ELECTRON MICROSCOPY (6.6 Å)