6TMF

Structure of an archaeal ABCE1-bound ribosomal post-splitting complex

Summary for 6TMF

• Entry DOI: 10.2210/pdb6tmf/pdb
• EMDB information: 10519
• Descriptor: 16S ribosomal RNA, 30S ribosomal protein S8, 30S ribosomal protein S8e, ... (34 entities in total)
• Functional Keywords: abc proteins, ribosome recycling, translation, ribosome
• Biological source: Saccharolobus solfataricus; More
• Total number of polymer chains: 30
• Total formula weight: 962388.30

Authors

Kratzat, H.,Becker, T.,Tampe, R.,Beckmann, R. (deposition date: 2019-12-04, release date: 2020-02-12, Last modification date: 2024-05-22)

Primary citation

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

PubMed 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.

PubMed: 32064661
DOI: 10.15252/embj.2019103788

Experimental method

ELECTRON MICROSCOPY (2.8 Å)