7O5B

Cryo-EM structure of a Bacillus subtilis MifM-stalled ribosome-nascent chain complex with (p)ppGpp-SRP bound

This is a non-PDB format compatible entry.

Summary for 7O5B

• Entry DOI: 10.2210/pdb7o5b/pdb
• EMDB information: 12734
• Descriptor: tRNA, 50S ribosomal protein L2, 50S ribosomal protein L3, ... (57 entities in total)
• Functional Keywords: signal recognition particle co-translational targeting alarmones translation gtpases stress response, ribosome
• Biological source: Bacillus subtilis subsp. subtilis str. 168; More
• Total number of polymer chains: 56
• Total formula weight: 2295475.42

Authors

Kratzat, H.,Czech, L.,Berninghausen, O.,Bange, G.,Beckmann, R. (deposition date: 2021-04-08, release date: 2022-02-02, Last modification date: 2024-10-23)

Primary citation

Czech, L.,Mais, C.N.,Kratzat, H.,Sarmah, P.,Giammarinaro, P.,Freibert, S.A.,Esser, H.F.,Musial, J.,Berninghausen, O.,Steinchen, W.,Beckmann, R.,Koch, H.G.,Bange, G.
Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp.
Nat Commun, 13:1069-1069, 2022

PubMed Abstract: The stringent response enables bacteria to respond to nutrient limitation and other stress conditions through production of the nucleotide-based second messengers ppGpp and pppGpp, collectively known as (p)ppGpp. Here, we report that (p)ppGpp inhibits the signal recognition particle (SRP)-dependent protein targeting pathway, which is essential for membrane protein biogenesis and protein secretion. More specifically, (p)ppGpp binds to the SRP GTPases Ffh and FtsY, and inhibits the formation of the SRP receptor-targeting complex, which is central for the coordinated binding of the translating ribosome to the SecYEG translocon. Cryo-EM analysis of SRP bound to translating ribosomes suggests that (p)ppGpp may induce a distinct conformational stabilization of the NG domain of Ffh and FtsY in Bacillus subtilis but not in E. coli.

PubMed: 35217658
DOI: 10.1038/s41467-022-28675-0

Experimental method

ELECTRON MICROSCOPY (3.33 Å)