6HTQ
Stringent response control by a bifunctional RelA enzyme in the presence and absence of the ribosome
This is a non-PDB format compatible entry.
Summary for 6HTQ
| Entry DOI | 10.2210/pdb6htq/pdb |
| EMDB information | 0270 |
| Descriptor | 23S ribosomal RNA, 50S ribosomal protein L15, 50S ribosomal protein L16, ... (53 entities in total) |
| Functional Keywords | structure of bifunctional rel on b. subtilis 70s, ribosome |
| Biological source | Bacillus subtilis subsp. subtilis str. 168 More |
| Total number of polymer chains | 53 |
| Total formula weight | 2190608.52 |
| Authors | Wilson, D.N.,Abdelshahid, M. (deposition date: 2018-10-04, release date: 2019-10-23, Last modification date: 2024-10-16) |
| Primary citation | Pausch, P.,Abdelshahid, M.,Steinchen, W.,Schafer, H.,Gratani, F.L.,Freibert, S.A.,Wolz, C.,Turgay, K.,Wilson, D.N.,Bange, G. Structural Basis for Regulation of the Opposing (p)ppGpp Synthetase and Hydrolase within the Stringent Response Orchestrator Rel. Cell Rep, 32:108157-108157, 2020 Cited by PubMed Abstract: The stringent response enables metabolic adaptation of bacteria under stress conditions and is governed by RelA/SpoT Homolog (RSH)-type enzymes. Long RSH-type enzymes encompass an N-terminal domain (NTD) harboring the second messenger nucleotide (p)ppGpp hydrolase and synthetase activity and a stress-perceiving and regulatory C-terminal domain (CTD). CTD-mediated binding of Rel to stalled ribosomes boosts (p)ppGpp synthesis. However, how the opposing activities of the NTD are controlled in the absence of stress was poorly understood. Here, we demonstrate on the RSH-type protein Rel that the critical regulative elements reside within the TGS (ThrRS, GTPase, and SpoT) subdomain of the CTD, which associates to and represses the synthetase to concomitantly allow for activation of the hydrolase. Furthermore, we show that Rel forms homodimers, which appear to control the interaction with deacylated-tRNA, but not the enzymatic activity of Rel. Collectively, our study provides a detailed molecular view into the mechanism of stringent response repression in the absence of stress. PubMed: 32937119DOI: 10.1016/j.celrep.2020.108157 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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