6VYZ
Escherichia coli transcription-translation complex C6 (TTC-C6) containing mRNA with a 21 nt long spacer, NusA, and fMet-tRNAs at E-site and P-site
This is a non-PDB format compatible entry.
Summary for 6VYZ
| Entry DOI | 10.2210/pdb6vyz/pdb |
| EMDB information | 21477 |
| Descriptor | 50S ribosomal protein L21, DNA-directed RNA polymerase subunit beta, Transcription termination/antitermination protein NusG, ... (65 entities in total) |
| Functional Keywords | bacterial coupled transcription-translation complex, transcription, ribosome, transcription-translation complex, transcription/translation |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 65 |
| Total formula weight | 2692567.22 |
| Authors | Molodtsov, V.,Wang, C.,Su, M.,Ebright, R.H. (deposition date: 2020-02-27, release date: 2020-09-02, Last modification date: 2024-11-13) |
| Primary citation | Wang, C.,Molodtsov, V.,Firlar, E.,Kaelber, J.T.,Blaha, G.,Su, M.,Ebright, R.H. Structural basis of transcription-translation coupling. Science, 369:1359-1365, 2020 Cited by PubMed Abstract: In bacteria, transcription and translation are coupled processes in which the movement of RNA polymerase (RNAP)-synthesizing messenger RNA (mRNA) is coordinated with the movement of the first ribosome-translating mRNA. Coupling is modulated by the transcription factors NusG (which is thought to bridge RNAP and the ribosome) and NusA. Here, we report cryo-electron microscopy structures of transcription-translation complexes (TTCs) containing different-length mRNA spacers between RNAP and the ribosome active-center P site. Structures of TTCs containing short spacers show a state incompatible with NusG bridging and NusA binding (TTC-A, previously termed "expressome"). Structures of TTCs containing longer spacers reveal a new state compatible with NusG bridging and NusA binding (TTC-B) and reveal how NusG bridges and NusA binds. We propose that TTC-B mediates NusG- and NusA-dependent transcription-translation coupling. PubMed: 32820061DOI: 10.1126/science.abb5317 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (9.9 Å) |
Structure validation
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