6LDI
The cryo-EM structure of E. coli CueR transcription activation complex
Summary for 6LDI
| Entry DOI | 10.2210/pdb6ldi/pdb |
| EMDB information | 0874 |
| Descriptor | DNA-directed RNA polymerase subunit alpha, ZINC ION, MAGNESIUM ION, ... (12 entities in total) |
| Functional Keywords | rna polymerase, cuer, transcription activation, transcription, transcription (dna to rna) |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 11 |
| Total formula weight | 527205.42 |
| Authors | Fang, C.L.,Zhang, Y. (deposition date: 2019-11-21, release date: 2020-09-30, Last modification date: 2024-03-27) |
| Primary citation | Fang, C.,Philips, S.J.,Wu, X.,Chen, K.,Shi, J.,Shen, L.,Xu, J.,Feng, Y.,O'Halloran, T.V.,Zhang, Y. CueR activates transcription through a DNA distortion mechanism. Nat.Chem.Biol., 17:57-64, 2021 Cited by PubMed Abstract: The MerR-family transcription factors (TFs) are a large group of bacterial proteins responding to cellular metal ions and multiple antibiotics by binding within central RNA polymerase-binding regions of a promoter. While most TFs alter transcription through protein-protein interactions, MerR TFs are capable of reshaping promoter DNA. To address the question of which mechanism prevails, we determined two cryo-EM structures of transcription activation complexes (TAC) comprising Escherichia coli CueR (a prototype MerR TF), RNAP holoenzyme and promoter DNA. The structures reveal that this TF promotes productive promoter-polymerase association without canonical protein-protein contacts seen between other activator proteins and RNAP. Instead, CueR realigns the key promoter elements in the transcription activation complex by clamp-like protein-DNA interactions: these induce four distinct kinks that ultimately position the -10 element for formation of the transcription bubble. These structural and biochemical results provide strong support for the DNA distortion paradigm of allosteric transcriptional control by MerR TFs. PubMed: 32989300DOI: 10.1038/s41589-020-00653-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.69 Å) |
Structure validation
Download full validation report
