7CKQ
The cryo-EM structure of B. subtilis BmrR transcription activation complex
Summary for 7CKQ
| Entry DOI | 10.2210/pdb7ckq/pdb |
| EMDB information | 30390 |
| Descriptor | DNA-directed RNA polymerase subunit alpha, MAGNESIUM ION, ZINC ION, ... (12 entities in total) |
| Functional Keywords | rna polymerase, transcription activation, transcription |
| Biological source | Bacillus subtilis (strain 168) More |
| Total number of polymer chains | 11 |
| Total formula weight | 494728.47 |
| Authors | Fang, C.L.,Zhang, Y. (deposition date: 2020-07-18, release date: 2020-12-16, Last modification date: 2024-03-27) |
| Primary citation | Fang, C.,Li, L.,Zhao, Y.,Wu, X.,Philips, S.J.,You, L.,Zhong, M.,Shi, X.,O'Halloran, T.V.,Li, Q.,Zhang, Y. The bacterial multidrug resistance regulator BmrR distorts promoter DNA to activate transcription. Nat Commun, 11:6284-6284, 2020 Cited by PubMed Abstract: The MerR-family proteins represent a unique family of bacteria transcription factors (TFs), which activate transcription in a manner distinct from canonical ones. Here, we report a cryo-EM structure of a B. subtilis transcription activation complex comprising B. subtilis six-subunit (2αββ'ωε) RNA Polymerase (RNAP) core enzyme, σ, a promoter DNA, and the ligand-bound B. subtilis BmrR, a prototype of MerR-family TFs. The structure reveals that RNAP and BmrR recognize the upstream promoter DNA from opposite faces and induce four significant kinks from the -35 element to the -10 element of the promoter DNA in a cooperative manner, which restores otherwise inactive promoter activity by shortening the length of promoter non-optimal -35/-10 spacer. Our structure supports a DNA-distortion and RNAP-non-contact paradigm of transcriptional activation by MerR TFs. PubMed: 33293519DOI: 10.1038/s41467-020-20134-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.4 Å) |
Structure validation
Download full validation report
