9ZNF

Cryo-EM structure of the Methanosarcina acetivorans 70S ribosome in complex with SriA and SriB

This is a non-PDB format compatible entry.

Summary for 9ZNF

• Entry DOI: 10.2210/pdb9znf/pdb
• EMDB information: 74446
• Descriptor: 23S rRNA, Large ribosomal subunit protein uL5, Large ribosomal subunit protein uL6, ... (65 entities in total)
• Functional Keywords: ribosome, hibernation, archaea
• Biological source: Methanosarcina acetivorans; More
• Total number of polymer chains: 62
• Total formula weight: 2410814.32

Authors

Nissley, A.J.,Cate, J.H.D. (deposition date: 2025-12-12, release date: 2026-01-28, Last modification date: 2026-04-08)

Primary citation

Nissley, A.J.,Williams, M.C.,Shulgina, Y.,Kivimae, R.W.,Nayak, D.D.,Cate, J.H.D.
A family of archaeal hibernation factors that bind in tandem and protect ribosomes in dormant cells.
Biorxiv, 2026

PubMed Abstract: Under nutrient limitation or stress, ribosome hibernation factors inactivate and protect ribosomes. Although ribosome hibernation plays an important role in microbes, we lack a complete understanding of this process in archaea. Here, we identify a family of hibernation factors, which we designate as single ribosomal subunit inhibitors (SriA-SriD), from the methanogenic archaeon . All four genes are encoded in an operon and each Sri protein inhibits protein synthesis . Deletion of genes in impaired growth recovery after prolonged stationary phase and also led to depletion of the small ribosomal subunit. Cryo-EM structures show that Sri proteins bind to the ribosome in tandem and form conserved protein-protein interfaces. Sri is broadly distributed across archaeal phyla and genes frequently co-occur. Together, these findings establish Sri proteins as a distinct group of hibernation factors that protect ribosomes during dormancy and expand our understanding of ribosome hibernation in archaea.

PubMed: 41867869
DOI: 10.64898/2026.01.19.700200

Experimental method

ELECTRON MICROSCOPY (2.03 Å)