SNAP output for PDB entry 3j16 [SNAP web server]

PDB-id

3j16; SNAP-derived features in text and JSON formats; DNAproDB

Class

ribosome

Method

cryo-EM (7.2 Å)

Summary

Models of ribosome-bound dom34p and rli1p and their ribosomal binding partners

Reference

Becker T, Franckenberg S, Wickles S, Shoemaker CJ, Anger AM, Armache J-P, Sieber H, Ungewickell C, Berninghausen O, Daberkow I, Karcher A, Thomm M, Hopfner KP, Green R, Beckmann R (2012): "Structural basis of highly conserved ribosome recycling in eukaryotes and archaea." Nature, 482, 501-506. doi: 10.1038/nature10829.

Abstract

Ribosome-driven protein biosynthesis is comprised of four phases: initiation, elongation, termination and recycling. In bacteria, ribosome recycling requires ribosome recycling factor and elongation factor G, and several structures of bacterial recycling complexes have been determined. In the eukaryotic and archaeal kingdoms, however, recycling involves the ABC-type ATPase ABCE1 and little is known about its structural basis. Here we present cryo-electron microscopy reconstructions of eukaryotic and archaeal ribosome recycling complexes containing ABCE1 and the termination factor paralogue Pelota. These structures reveal the overall binding mode of ABCE1 to be similar to canonical translation factors. Moreover, the iron-sulphur cluster domain of ABCE1 interacts with and stabilizes Pelota in a conformation that reaches towards the peptidyl transferase centre, thus explaining how ABCE1 may stimulate peptide-release activity of canonical termination factors. Using the mechanochemical properties of ABCE1, a conserved mechanism in archaea and eukaryotes is suggested that couples translation termination to recycling, and eventually to re-initiation.