6FXC

The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus

This is a non-PDB format compatible entry.

Replaces:  5NG8

Summary for 6FXC

• Entry DOI: 10.2210/pdb6fxc/pdb
• EMDB information: 3637
• Descriptor: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (52 entities in total)
• Functional Keywords: ribosome cryo-em structural biology hibernation, ribosome
• Biological source: Staphylococcus aureus; More
• Total number of polymer chains: 104
• Total formula weight: 4236804.35

Authors

Matzov, D.,Aibara, S.,Zimmerman, E.,Bashan, A.,Kidmose, R.,Amunts, A.,Yonath, A. (deposition date: 2018-03-08, release date: 2018-03-21, Last modification date: 2024-10-16)

Primary citation

Matzov, D.,Aibara, S.,Basu, A.,Zimmerman, E.,Bashan, A.,Yap, M.F.,Amunts, A.,Yonath, A.E.
The cryo-EM structure of hibernating 100S ribosome dimer from pathogenic Staphylococcus aureus.
Nat Commun, 8:723-723, 2017

PubMed Abstract: Formation of 100S ribosome dimer is generally associated with translation suppression in bacteria. Trans-acting factors ribosome modulation factor (RMF) and hibernating promoting factor (HPF) were shown to directly mediate this process in E. coli. Gram-positive S. aureus lacks an RMF homolog and the structural basis for its 100S formation was not known. Here we report the cryo-electron microscopy structure of the native 100S ribosome from S. aureus, revealing the molecular mechanism of its formation. The structure is distinct from previously reported analogs and relies on the HPF C-terminal extension forming the binding platform for the interactions between both of the small ribosomal subunits. The 100S dimer is formed through interactions between rRNA h26, h40, and protein uS2, involving conformational changes of the head as well as surface regions that could potentially prevent RNA polymerase from docking to the ribosome.Under conditions of nutrient limitation, bacterial ribosomes undergo dimerization, forming a 100S complex that is translationally inactive. Here the authors present the structural basis for formation of the 100S complexes in Gram-positive bacteria, shedding light on the mechanism of translation suppression by the ribosome-silencing factors.

PubMed: 28959035
DOI: 10.1038/s41467-017-00753-8

Experimental method

ELECTRON MICROSCOPY (6.76 Å)