Structure of the 70 <i>S</i> Ribosome Complexed with mRNA and tRNA

TLDR

The bacterial 70S ribosome’s E‑site tRNA interactions with the 50S subunit show both similarities and differences relative to archaeal ribosomes. The 2.8‑Å crystal structure of the bacterial 70S ribosome reveals atomic details of mRNA and tRNA interactions, including a metal‑ion‑stabilized kink that separates the A and P sites to prevent mRNA slippage and a metal‑ion‑stabilized intersubunit interface, thereby explaining many biochemical and genetic observations.

Abstract

The crystal structure of the bacterial 70S ribosome refined to 2.8 angstrom resolution reveals atomic details of its interactions with messenger RNA (mRNA) and transfer RNA (tRNA). A metal ion stabilizes a kink in the mRNA that demarcates the boundary between A and P sites, which is potentially important to prevent slippage of mRNA. Metal ions also stabilize the intersubunit interface. The interactions of E-site tRNA with the 50S subunit have both similarities and differences compared to those in the archaeal ribosome. The structure also rationalizes much biochemical and genetic data on translation.