8E5K
Escherichia coli Rho-dependent transcription pre-termination complex containing 21 nt long RNA spacer, Mg-ADP-BeF3, and NusG; TEC part
Summary for 8E5K
| Entry DOI | 10.2210/pdb8e5k/pdb |
| EMDB information | 27864 27865 27913 27914 27915 27916 27917 27918 |
| Descriptor | NT DNA, ZINC ION, T DNA, ... (10 entities in total) |
| Functional Keywords | factor-dependent termination, rho, transcription termination, transcription elongation complex, helicase, atpase, transcription, transferase-dna-rna complex, transferase/dna/rna |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 9 |
| Total formula weight | 459088.63 |
| Authors | Molodtsov, V.,Wang, C. (deposition date: 2022-08-22, release date: 2022-09-07, Last modification date: 2024-11-13) |
| Primary citation | Molodtsov, V.,Wang, C.,Firlar, E.,Kaelber, J.T.,Ebright, R.H. Structural basis of Rho-dependent transcription termination. Nature, 614:367-374, 2023 Cited by PubMed Abstract: Rho is a ring-shaped hexameric ATP-dependent molecular motor. Together with the transcription elongation factor NusG, Rho mediates factor-dependent transcription termination and transcription-translation-coupling quality control in Escherichia coli. Here we report the preparation of complexes that are functional in factor-dependent transcription termination from Rho, NusG, RNA polymerase (RNAP), and synthetic nucleic acid scaffolds, and we report cryogenic electron microscopy structures of the complexes. The structures show that functional factor-dependent pre-termination complexes contain a closed-ring Rho hexamer; have RNA threaded through the central channel of Rho; have 60 nucleotides of RNA interacting sequence-specifically with the exterior of Rho and 6 nucleotides of RNA interacting sequence-specifically with the central channel of Rho; have Rho oriented relative to RNAP such that ATP-dependent translocation by Rho exerts mechanical force on RNAP; and have NusG bridging Rho and RNAP. The results explain five decades of research on Rho and provide a foundation for understanding Rho's function. PubMed: 36697824DOI: 10.1038/s41586-022-05658-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.2 Å) |
Structure validation
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