5VT0
Escherichia coli 6S RNA derivative in complex with Escherichia coli RNA polymerase sigma70-holoenzyme
Summary for 5VT0
Entry DOI | 10.2210/pdb5vt0/pdb |
EMDB information | 8732 |
Descriptor | DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (8 entities in total) |
Functional Keywords | rnap, 6s rna, ncrna, transcription regulation, transcription-rna complex, transcription/rna |
Biological source | Escherichia coli (strain K12) More |
Total number of polymer chains | 7 |
Total formula weight | 476027.19 |
Authors | Chen, J.,Darst, S.A. (deposition date: 2017-05-15, release date: 2017-11-01, Last modification date: 2024-03-13) |
Primary citation | Chen, J.,Wassarman, K.M.,Feng, S.,Leon, K.,Feklistov, A.,Winkelman, J.T.,Li, Z.,Walz, T.,Campbell, E.A.,Darst, S.A. 6S RNA Mimics B-Form DNA to Regulate Escherichia coli RNA Polymerase. Mol. Cell, 68:388-397.e6, 2017 Cited by PubMed Abstract: Noncoding RNAs (ncRNAs) regulate gene expression in all organisms. Bacterial 6S RNAs globally regulate transcription by binding RNA polymerase (RNAP) holoenzyme and competing with promoter DNA. Escherichia coli (Eco) 6S RNA interacts specifically with the housekeeping σ-holoenzyme (Eσ) and plays a key role in the transcriptional reprogramming upon shifts between exponential and stationary phase. Inhibition is relieved upon 6S RNA-templated RNA synthesis. We report here the 3.8 Å resolution structure of a complex between 6S RNA and Eσ determined by single-particle cryo-electron microscopy and validation of the structure using footprinting and crosslinking approaches. Duplex RNA segments have A-form C3' endo sugar puckers but widened major groove widths, giving the RNA an overall architecture that mimics B-form promoter DNA. Our results help explain the specificity of Eco 6S RNA for Eσ and show how an ncRNA can mimic B-form DNA to directly regulate transcription by the DNA-dependent RNAP. PubMed: 28988932DOI: 10.1016/j.molcel.2017.09.006 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.78 Å) |
Structure validation
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