SNAP annotations: PDB entry 6tmf

PDB-id

6tmf; DSSR-derived features in text and JSON formats; DNAproDB

Class

ribosome

Method

cryo-EM (2.8 Å)

Summary

Structure of an archaeal abce1-bound ribosomal post-splitting complex

Reference

Nurenberg-Goloub E, Kratzat H, Heinemann H, Heuer A, Kotter P, Berninghausen O, Becker T, Tampe R, Beckmann R (2020): "Molecular analysis of the ribosome recycling factor ABCE1 bound to the 30S post-splitting complex." Embo J., 39, e103788. doi: 10.15252/embj.2019103788.

Abstract

Ribosome recycling by the twin-ATPase ABCE1 is a key regulatory process in mRNA translation and surveillance and in ribosome-associated protein quality control in Eukarya and Archaea. Here, we captured the archaeal 30S ribosome post-splitting complex at 2.8 Å resolution by cryo-electron microscopy. The structure reveals the dynamic behavior of structural motifs unique to ABCE1, which ultimately leads to ribosome splitting. More specifically, we provide molecular details on how conformational rearrangements of the iron-sulfur cluster domain and hinge regions of ABCE1 are linked to closure of its nucleotide-binding sites. The combination of mutational and functional analyses uncovers an intricate allosteric network between the ribosome, regulatory domains of ABCE1, and its two structurally and functionally asymmetric ATP-binding sites. Based on these data, we propose a refined model of how signals from the ribosome are integrated into the ATPase cycle of ABCE1 to orchestrate ribosome recycling.