8FTD
Structure of Escherichia coli CedA in complex with transcription initiation complex
Summary for 8FTD
| Entry DOI | 10.2210/pdb8ftd/pdb |
| EMDB information | 29423 |
| Descriptor | DNA-directed RNA polymerase subunit alpha, MAGNESIUM ION, ZINC ION, ... (11 entities in total) |
| Functional Keywords | escherichia coli, ceda, initiation complex, transcription, transferase-dna complex, transferase/dna |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 10 |
| Total formula weight | 559830.07 |
| Authors | Liu, M.,Vassyliev, N.,Nudler, E. (deposition date: 2023-01-11, release date: 2024-01-10, Last modification date: 2024-01-31) |
| Primary citation | Vasilyev, N.,Liu, M.M.J.,Epshtein, V.,Shamovsky, I.,Nudler, E. General transcription factor from Escherichia coli with a distinct mechanism of action. Nat.Struct.Mol.Biol., 31:141-149, 2024 Cited by PubMed Abstract: Gene expression in Escherichia coli is controlled by well-established mechanisms that activate or repress transcription. Here, we identify CedA as an unconventional transcription factor specifically associated with the RNA polymerase (RNAP) σ holoenzyme. Structural and biochemical analysis of CedA bound to RNAP reveal that it bridges distant domains of β and σ subunits to stabilize an open-promoter complex. CedA does so without contacting DNA. We further show that cedA is strongly induced in response to amino acid starvation, oxidative stress and aminoglycosides. CedA provides a basal level of tolerance to these clinically relevant antibiotics, as well as to rifampicin and peroxide. Finally, we show that CedA modulates transcription of hundreds of bacterial genes, which explains its pleotropic effect on cell physiology and pathogenesis. PubMed: 38177674DOI: 10.1038/s41594-023-01154-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.76 Å) |
Structure validation
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