4V8G

Crystal structure of RMF bound to the 70S ribosome.

This is a non-PDB format compatible entry.

Summary for 4V8G

• Entry DOI: 10.2210/pdb4v8g/pdb
• Descriptor: 16S Ribosomal RNA, 30S Ribosomal Protein S10, 30S Ribosomal Protein S11, ... (56 entities in total)
• Functional Keywords: ribosome modulation factor, stress response, small subunit head movement, stationary phase, ribosome hibernation, ribosome
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm : P0AFW2
• Total number of polymer chains: 106
• Total formula weight: 4384335.21

Authors

Polikanov, Y.S.,Blaha, G.M.,Steitz, T.A. (deposition date: 2011-12-11, release date: 2014-07-09, Last modification date: 2024-11-06)

Primary citation

Polikanov, Y.S.,Blaha, G.M.,Steitz, T.A.
How hibernation factors RMF, HPF, and YfiA turn off protein synthesis.
Science, 336:915-918, 2012

PubMed Abstract: Eubacteria inactivate their ribosomes as 100S dimers or 70S monomers upon entry into stationary phase. In Escherichia coli, 100S dimer formation is mediated by ribosome modulation factor (RMF) and hibernation promoting factor (HPF), or alternatively, the YfiA protein inactivates ribosomes as 70S monomers. Here, we present high-resolution crystal structures of the Thermus thermophilus 70S ribosome in complex with each of these stationary-phase factors. The binding site of RMF overlaps with that of the messenger RNA (mRNA) Shine-Dalgarno sequence, which prevents the interaction between the mRNA and the 16S ribosomal RNA. The nearly identical binding sites of HPF and YfiA overlap with those of the mRNA, transfer RNA, and initiation factors, which prevents translation initiation. The binding of RMF and HPF, but not YfiA, to the ribosome induces a conformational change of the 30S head domain that promotes 100S dimer formation.

PubMed: 22605777
DOI: 10.1126/science.1218538

Experimental method

X-RAY DIFFRACTION (3 Å)