7N2C

Elongating 70S ribosome complex in a fusidic acid-stalled intermediate state of translocation bound to EF-G(GDP) (INT2)

これはPDB形式変換不可エントリーです。

7N2C の概要

• エントリーDOI: 10.2210/pdb7n2c/pdb
• EMDBエントリー: 24132
• 分子名称: 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (68 entities in total)
• 機能のキーワード: elongation complex, trna, mrna, ribosome
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 61
• 化学式量合計: 2363631.14

構造登録者

Rundlet, E.J.,Holm, M.,Schacherl, M.,Natchiar, K.S.,Altman, R.B.,Spahn, C.M.T.,Myasnikov, A.G.,Blanchard, S.C. (登録日: 2021-05-28, 公開日: 2021-07-14, 最終更新日: 2025-03-19)

主引用文献

Rundlet, E.J.,Holm, M.,Schacherl, M.,Natchiar, S.K.,Altman, R.B.,Spahn, C.M.T.,Myasnikov, A.G.,Blanchard, S.C.
Structural basis of early translocation events on the ribosome.
Nature, 595:741-745, 2021

PubMed Abstract: Peptide-chain elongation during protein synthesis entails sequential aminoacyl-tRNA selection and translocation reactions that proceed rapidly (2-20 per second) and with a low error rate (around 10 to 10 at each step) over thousands of cycles. The cadence and fidelity of ribosome transit through mRNA templates in discrete codon increments is a paradigm for movement in biological systems that must hold for diverse mRNA and tRNA substrates across domains of life. Here we use single-molecule fluorescence methods to guide the capture of structures of early translocation events on the bacterial ribosome. Our findings reveal that the bacterial GTPase elongation factor G specifically engages spontaneously achieved ribosome conformations while in an active, GTP-bound conformation to unlock and initiate peptidyl-tRNA translocation. These findings suggest that processes intrinsic to the pre-translocation ribosome complex can regulate the rate of protein synthesis, and that energy expenditure is used later in the translocation mechanism than previously proposed.

PubMed: 34234344
DOI: 10.1038/s41586-021-03713-x

実験手法

ELECTRON MICROSCOPY (2.72 Å)