7O9G
Escherichia coli Ffh in complex with ppGpp
Summary for 7O9G
| Entry DOI | 10.2210/pdb7o9g/pdb |
| Descriptor | Signal recognition particle protein, GUANOSINE-5',3'-TETRAPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | stringent response, targeting complex, signal recognition particle, alarmones, stress, translation |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 34022.93 |
| Authors | Czech, L.,Mais, C.-N.,Bange, G. (deposition date: 2021-04-16, release date: 2022-02-02, Last modification date: 2024-01-31) |
| 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 Cited by 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: 35217658DOI: 10.1038/s41467-022-28675-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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