6GZQ

T. thermophilus hibernating 70S ribosome

This is a non-PDB format compatible entry.

Summary for 6GZQ

• Entry DOI: 10.2210/pdb6gzq/pdb
• EMDB information: 0101
• Descriptor: 50S ribosomal protein L2, 50S ribosomal protein L16, 50S ribosomal protein L17, ... (53 entities in total)
• Functional Keywords: ribosome, hibernation, 100s dimer, cryo-em
• Biological source: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579); More
• Total number of polymer chains: 53
• Total formula weight: 2135989.85

Authors

Flygaard, R.K.,Jenner, L.B. (deposition date: 2018-07-04, release date: 2018-10-24, Last modification date: 2024-11-13)

Primary citation

Flygaard, R.K.,Boegholm, N.,Yusupov, M.,Jenner, L.B.
Cryo-EM structure of the hibernating Thermus thermophilus 100S ribosome reveals a protein-mediated dimerization mechanism.
Nat Commun, 9:4179-4179, 2018

PubMed Abstract: In response to cellular stresses bacteria conserve energy by dimerization of ribosomes into inactive hibernating 100S ribosome particles. Ribosome dimerization in Thermus thermophilus is facilitated by hibernation-promoting factor (TtHPF). In this study we demonstrate high sensitivity of Tt100S formation to the levels of TtHPF and show that a 1:1 ratio leads to optimal dimerization. We report structures of the T. thermophilus 100S ribosome determined by cryo-electron microscopy to average resolutions of 4.13 Å and 4.57 Å. In addition, we present a 3.28 Å high-resolution cryo-EM reconstruction of a 70S ribosome from a hibernating ribosome dimer and reveal a role for the linker region connecting the TtHPF N- and C-terminal domains in translation inhibition by preventing Shine-Dalgarno duplex formation. Our work demonstrates that species-specific differences in the dimerization interface govern the overall conformation of the 100S ribosome particle and that for Thermus thermophilus no ribosome-ribosome interactions are involved in the interface.

PubMed: 30301898
DOI: 10.1038/s41467-018-06724-x

Experimental method

ELECTRON MICROSCOPY (3.28 Å)