6B6H
The cryo-EM structure of a bacterial class I transcription activation complex
Summary for 6B6H
| Entry DOI | 10.2210/pdb6b6h/pdb |
| EMDB information | 7059 7060 |
| Descriptor | DNA-directed RNA polymerase subunit alpha, NASCENT RNA 3-MER, ZINC ION, ... (13 entities in total) |
| Functional Keywords | transcription, rna polymerase, catabolite activator protein, camp, transcription-transferase-dna-rna complex, transcription/transferase/dna/rna |
| Biological source | Escherichia coli O157:H7 More |
| Total number of polymer chains | 12 |
| Total formula weight | 573751.36 |
| Authors | Liu, B.,Hong, C.,Huang, R.,Yu, Z.,Steitz, T.A. (deposition date: 2017-10-02, release date: 2017-11-15, Last modification date: 2024-03-13) |
| Primary citation | Liu, B.,Hong, C.,Huang, R.K.,Yu, Z.,Steitz, T.A. Structural basis of bacterial transcription activation. Science, 358:947-951, 2017 Cited by PubMed Abstract: In bacteria, the activation of gene transcription at many promoters is simple and only involves a single activator. The cyclic adenosine 3',5'-monophosphate receptor protein (CAP), a classic activator, is able to activate transcription independently through two different mechanisms. Understanding the class I mechanism requires an intact transcription activation complex (TAC) structure at a high resolution. Here we report a high-resolution cryo-electron microscopy structure of an intact class I TAC containing a CAP dimer, a σ-RNA polymerase (RNAP) holoenzyme, a complete class I CAP-dependent promoter DNA, and a de novo synthesized RNA oligonucleotide. The structure shows how CAP wraps the upstream DNA and how the interactions recruit RNAP. Our study provides a structural basis for understanding how activators activate transcription through the class I recruitment mechanism. PubMed: 29146813DOI: 10.1126/science.aao1923 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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