6DUQ
Structure of a Rho-NusG KOW domain complex
Summary for 6DUQ
| Entry DOI | 10.2210/pdb6duq/pdb |
| Descriptor | Transcription termination factor Rho, Transcription termination/antitermination protein NusG, rU12, ... (6 entities in total) |
| Functional Keywords | rho, nusg, reca, atpase, transcription, transcription-rna complex, transcription/rna |
| Biological source | Escherichia coli M718 More |
| Total number of polymer chains | 26 |
| Total formula weight | 662115.81 |
| Authors | Berger, J.M.,Lawson, M.R. (deposition date: 2018-06-21, release date: 2018-09-05, Last modification date: 2024-03-13) |
| Primary citation | Lawson, M.R.,Ma, W.,Bellecourt, M.J.,Artsimovitch, I.,Martin, A.,Landick, R.,Schulten, K.,Berger, J.M. Mechanism for the Regulated Control of Bacterial Transcription Termination by a Universal Adaptor Protein. Mol. Cell, 71:911-922.e4, 2018 Cited by PubMed Abstract: NusG/Spt5 proteins are the only transcription factors utilized by all cellular organisms. In enterobacteria, NusG antagonizes the transcription termination activity of Rho, a hexameric helicase, during the synthesis of ribosomal and actively translated mRNAs. Paradoxically, NusG helps Rho act on untranslated transcripts, including non-canonical antisense RNAs and those arising from translational stress; how NusG fulfills these disparate functions is unknown. Here, we demonstrate that NusG activates Rho by assisting helicase isomerization from an open-ring, RNA-loading state to a closed-ring, catalytically active translocase. A crystal structure of closed-ring Rho in complex with NusG reveals the physical basis for this activation and further explains how Rho is excluded from translationally competent RNAs. This study demonstrates how a universally conserved transcription factor acts to modulate the activity of a ring-shaped ATPase motor and establishes how the innate sequence bias of a termination factor can be modulated to silence pervasive, aberrant transcription. PubMed: 30122535DOI: 10.1016/j.molcel.2018.07.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.7 Å) |
Structure validation
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