7ADB
Transcription termination intermediate complex 1 delta NusG
Summary for 7ADB
| Entry DOI | 10.2210/pdb7adb/pdb |
| EMDB information | 11722 |
| Descriptor | Transcription termination factor Rho, BERYLLIUM TRIFLUORIDE ION, ADENOSINE-5'-DIPHOSPHATE, ... (14 entities in total) |
| Functional Keywords | rna polymerase, rho, transcription |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 15 |
| Total formula weight | 793396.90 |
| Authors | Said, N.,Hilal, T.,Loll, B.,Wahl, C.M. (deposition date: 2020-09-14, release date: 2020-11-04, Last modification date: 2021-02-03) |
| Primary citation | Said, N.,Hilal, T.,Sunday, N.D.,Khatri, A.,Burger, J.,Mielke, T.,Belogurov, G.A.,Loll, B.,Sen, R.,Artsimovitch, I.,Wahl, M.C. Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase rho. Science, 371:-, 2021 Cited by PubMed Abstract: Factor-dependent transcription termination mechanisms are poorly understood. We determined a series of cryo-electron microscopy structures portraying the hexameric adenosine triphosphatase (ATPase) ρ on a pathway to terminating NusA/NusG-modified elongation complexes. An open ρ ring contacts NusA, NusG, and multiple regions of RNA polymerase, trapping and locally unwinding proximal upstream DNA. NusA wedges into the ρ ring, initially sequestering RNA. Upon deflection of distal upstream DNA over the RNA polymerase zinc-binding domain, NusA rotates underneath one capping ρ subunit, which subsequently captures RNA. After detachment of NusG and clamp opening, RNA polymerase loses its grip on the RNA:DNA hybrid and is inactivated. Our structural and functional analyses suggest that ρ, and other termination factors across life, may use analogous strategies to allosterically trap transcription complexes in a moribund state. PubMed: 33243850DOI: 10.1126/science.abd1673 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.4 Å) |
Structure validation
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