8HSJ
Thermus thermophilus transcription termination factor Rho bound with ADP-BeF3
Summary for 8HSJ
| Entry DOI | 10.2210/pdb8hsj/pdb |
| Related | 8HSG 8HSH 8HSL 8HSR |
| EMDB information | 34996 34997 34999 35000 35004 |
| Descriptor | Transcription termination factor Rho, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | transcription termination, atp-dependent rna/dna helicase/translocase, transcription |
| Biological source | Thermus thermophilus HB8 |
| Total number of polymer chains | 6 |
| Total formula weight | 291082.70 |
| Authors | Murayama, Y.,Ehara, H.,Sekine, S. (deposition date: 2022-12-19, release date: 2023-05-03, Last modification date: 2024-07-03) |
| Primary citation | Murayama, Y.,Ehara, H.,Aoki, M.,Goto, M.,Yokoyama, T.,Sekine, S.I. Structural basis of the transcription termination factor Rho engagement with transcribing RNA polymerase from Thermus thermophilus. Sci Adv, 9:eade7093-eade7093, 2023 Cited by PubMed Abstract: Transcription termination is an essential step in transcription by RNA polymerase (RNAP) and crucial for gene regulation. For many bacterial genes, transcription termination is mediated by the adenosine triphosphate-dependent RNA translocase/helicase Rho, which causes RNA/DNA dissociation from the RNAP elongation complex (EC). However, the structural basis of the interplay between Rho and RNAP remains obscure. Here, we report the cryo-electron microscopy structure of the RNAP EC engaged with Rho. The Rho hexamer binds RNAP through the carboxyl-terminal domains, which surround the RNA exit site of RNAP, directing the nascent RNA seamlessly from the RNA exit to its central channel. The β-flap tip at the RNA exit is critical for the Rho-dependent RNA release, and its deletion causes an alternative Rho-RNAP binding mode, which is irrelevant to termination. The Rho binding site overlaps with the binding sites of other macromolecules, such as ribosomes, providing a general basis of gene regulation. PubMed: 36753546DOI: 10.1126/sciadv.ade7093 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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