8PIB
autoinhibited RfaH bound to E. coli transcription complex paused at ops site (encounter complex)
Summary for 8PIB
| Entry DOI | 10.2210/pdb8pib/pdb |
| Related | 8PDY 8PEN 8PFG 8PFJ 8PH9 8PHK 8PID 8PIL 8PIM |
| EMDB information | 17679 |
| Descriptor | Transcription antitermination protein RfaH, MAGNESIUM ION, DNA-directed RNA polymerase subunit beta, ... (10 entities in total) |
| Functional Keywords | pausing, encounter complex, rfah, ops site, transcription |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 9 |
| Total formula weight | 439357.88 |
| Authors | Zuber, P.K.,Said, N.,Hilal, T.,Loll, B.,Wahl, M.C.,Knauer, S.H. (deposition date: 2023-06-21, release date: 2024-04-24, Last modification date: 2024-10-23) |
| Primary citation | Zuber, P.K.,Said, N.,Hilal, T.,Wang, B.,Loll, B.,Gonzalez-Higueras, J.,Ramirez-Sarmiento, C.A.,Belogurov, G.A.,Artsimovitch, I.,Wahl, M.C.,Knauer, S.H. Concerted transformation of a hyper-paused transcription complex and its reinforcing protein. Nat Commun, 15:3040-3040, 2024 Cited by PubMed Abstract: RfaH, a paralog of the universally conserved NusG, binds to RNA polymerases (RNAP) and ribosomes to activate expression of virulence genes. In free, autoinhibited RfaH, an α-helical KOW domain sequesters the RNAP-binding site. Upon recruitment to RNAP paused at an ops site, KOW is released and refolds into a β-barrel, which binds the ribosome. Here, we report structures of ops-paused transcription elongation complexes alone and bound to the autoinhibited and activated RfaH, which reveal swiveled, pre-translocated pause states stabilized by an ops hairpin in the non-template DNA. Autoinhibited RfaH binds and twists the ops hairpin, expanding the RNA:DNA hybrid to 11 base pairs and triggering the KOW release. Once activated, RfaH hyper-stabilizes the pause, which thus requires anti-backtracking factors for escape. Our results suggest that the entire RfaH cycle is solely determined by the ops and RfaH sequences and provide insights into mechanisms of recruitment and metamorphosis of NusG homologs across all life. PubMed: 38589445DOI: 10.1038/s41467-024-47368-4 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
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