SNAP annotations: PDB entry 7asm

PDB-id

7asm; DSSR-derived features in text and JSON formats; DNAproDB

Class

ribosome

Method

cryo-EM (2.48 Å)

Summary

Staphylococcus aureus 50s after 30 minutes incubation at 37c

Reference

Cimicata G, Fridkin G, Bose T, Eyal Z, Halfon Y, Breiner-Goldstein E, Fox T, Zimmerman E, Bashan A, de Val N, Wlodawer A, Yonath A (2022): "Structural Studies Reveal the Role of Helix 68 in the Elongation Step of Protein Biosynthesis." Mbio, 13, e0030622. doi: 10.1128/mbio.00306-22.

Abstract

The ribosome, a multicomponent assembly consisting of RNA and proteins, is a pivotal macromolecular machine that translates the genetic code into proteins. The large ribosomal subunit rRNA helix 68 (H68) is a key element in the protein synthesis process, as it coordinates the coupled movements of the actors involved in translocation, including the tRNAs and L1 stalk. Examination of cryo-electron microscopy (cryo-EM) structures of ribosomes incubated for various time durations at physiological temperatures led to the identification of functionally relevant H68 movements. These movements assist the transition of the L1 stalk between its open and closed states. H68 spatial flexibility and its significance to the protein synthesis process were confirmed through its effective targeting with antisense PNA oligomers. Our results suggest that H68 is actively involved in ribosome movements that are central to the elongation process.