2RDO

50S subunit with EF-G(GDPNP) and RRF bound

2RDO の概要

• エントリーDOI: 10.2210/pdb2rdo/pdb
• 関連するPDBエントリー: 1EK8 1MZP 2AW4 2BM0
• EMDBエントリー: 1430
• 分子名称: 5S RIBOSOMAL RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (34 entities in total)
• 機能のキーワード: elongation factor g, ef-g, rrf, ribosome recycling factor, gdpnp, 50s subunit, cryo-em, real-space refinement, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, methylation, antibiotic resistance, repressor, transcription, transcription regulation, transcription termination, translation regulation, trna-binding, phosphoprotein, metal-binding, gtp-binding, nucleotide-binding, protein biosynthesis, ribosome
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 34
• 化学式量合計: 1477824.48

構造登録者

Gao, N.,Zavialov, A.V.,Ehrenberg, M.,Frank, J. (登録日: 2007-09-24, 公開日: 2008-03-04, 最終更新日: 2024-02-21)

主引用文献

Gao, N.,Zavialov, A.V.,Ehrenberg, M.,Frank, J.
Specific interaction between EF-G and RRF and its implication for GTP-dependent ribosome splitting into subunits.
J.Mol.Biol., 374:1345-1358, 2007

PubMed Abstract: After termination of protein synthesis, the bacterial ribosome is split into its 30S and 50S subunits by the action of ribosome recycling factor (RRF) and elongation factor G (EF-G) in a guanosine 5'-triphosphate (GTP)-hydrolysis-dependent manner. Based on a previous cryo-electron microscopy study of ribosomal complexes, we have proposed that the binding of EF-G to an RRF-containing posttermination ribosome triggers an interdomain rotation of RRF, which destabilizes two strong intersubunit bridges (B2a and B3) and, ultimately, separates the two subunits. Here, we present a 9-A (Fourier shell correlation cutoff of 0.5) cryo-electron microscopy map of a 50S x EF-G x guanosine 5'-[(betagamma)-imido]triphosphate x RRF complex and a quasi-atomic model derived from it, showing the interaction between EF-G and RRF on the 50S subunit in the presence of the noncleavable GTP analogue guanosine 5'-[(betagamma)-imido]triphosphate. The detailed information in this model and a comparative analysis of EF-G structures in various nucleotide- and ribosome-bound states show how rotation of the RRF head domain may be triggered by various domains of EF-G. For validation of our structural model, all known mutations in EF-G and RRF that relate to ribosome recycling have been taken into account. More importantly, our results indicate a substantial conformational change in the Switch I region of EF-G, suggesting that a conformational signal transduction mechanism, similar to that employed in transfer RNA translocation on the ribosome by EF-G, translates a large-scale movement of EF-G's domain IV, induced by GTP hydrolysis, into the domain rotation of RRF that eventually splits the ribosome into subunits.

PubMed: 17996252
DOI: 10.1016/j.jmb.2007.10.021

実験手法

ELECTRON MICROSCOPY (9.1 Å)