2KVQ
Solution structure of NusE:NusG-CTD complex
Summary for 2KVQ
| Entry DOI | 10.2210/pdb2kvq/pdb |
| NMR Information | BMRB: 16788 |
| Descriptor | NusE, Transcription antitermination protein nusG (2 entities in total) |
| Functional Keywords | nuse:nusg complex, transcription |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 2 |
| Total formula weight | 16563.98 |
| Authors | Burmann, B.M.,Schweimer, K.,Roesch, P. (deposition date: 2010-03-25, release date: 2010-05-05, Last modification date: 2024-05-22) |
| Primary citation | Burmann, B.M.,Schweimer, K.,Luo, X.,Wahl, M.C.,Stitt, B.L.,Gottesman, M.E.,Rosch, P. A NusE:NusG complex links transcription and translation. Science, 328:501-504, 2010 Cited by PubMed Abstract: Bacterial NusG is a highly conserved transcription factor that is required for most Rho activity in vivo. We show by nuclear magnetic resonance spectroscopy that Escherichia coli NusG carboxyl-terminal domain forms a complex alternatively with Rho or with transcription factor NusE, a protein identical to 30S ribosomal protein S10. Because NusG amino-terminal domain contacts RNA polymerase and the NusG carboxy-terminal domain interaction site of NusE is accessible in the ribosomal 30S subunit, NusG may act as a link between transcription and translation. Uncoupling of transcription and translation at the ends of bacterial operons enables transcription termination by Rho factor, and competition between ribosomal NusE and Rho for NusG helps to explain why Rho cannot terminate translated transcripts. PubMed: 20413501DOI: 10.1126/science.1184953 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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