9UKS
CryoEM structure of the T.thermophilus transcription initiation complex in the presence of Gp4A, -1 dA in the template DNA strand
Summary for 9UKS
| Entry DOI | 10.2210/pdb9uks/pdb |
| EMDB information | 64253 |
| Descriptor | DNA-directed RNA polymerase subunit alpha, ZINC ION, DNA-directed RNA polymerase subunit beta, ... (11 entities in total) |
| Functional Keywords | complex, transcription |
| Biological source | Thermus thermophilus HB8 More |
| Total number of polymer chains | 8 |
| Total formula weight | 457232.34 |
| Authors | Duan, W.,Kaushik, A.,Serganov, A. (deposition date: 2025-04-18, release date: 2025-10-22, Last modification date: 2025-10-29) |
| Primary citation | Duan, W.,Kaushik, A.,Unarta, I.C.,Wu, Y.,Liu, M.M.J.,Weaver, J.W.,Wang, B.,Rice, W.J.,Luciano, D.J.,Belasco, J.G.,Huang, X.,Nudler, E.,Serganov, A. Molecular basis for noncanonical transcription initiation from Np 4 A alarmones. Nat.Chem.Biol., 2025 Cited by PubMed Abstract: Stress-induced dinucleoside tetraphosphates (NpNs, where N is adenosine, guanosine, cytosine or uridine) are ubiquitous in living organisms, yet their function has been largely elusive for over 50 years. Recent studies have revealed that RNA polymerase can influence the cellular lifetime of transcripts by incorporating these alarmones into RNA as 5'-terminal caps. Here we present structural and biochemical data that reveal the molecular basis of noncanonical transcription initiation from NpAs by Escherichia coli and Thermus thermophilus RNA polymerases. Our results show the influence of the first two nucleotide incorporation steps on capping efficiency and the different interactions of NpAs with transcription initiation complexes. These data provide critical insights into the substrate selectivity that dictates levels of Np capping in bacterial cells. PubMed: 41094128DOI: 10.1038/s41589-025-02044-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.33 Å) |
Structure validation
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