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6GH6

Cryo-EM structure of bacterial RNA polymerase-sigma54 holoenzyme intermediate partially loaded complex

Summary for 6GH6
Entry DOI10.2210/pdb6gh6/pdb
EMDB information0002 4397
DescriptorDNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (7 entities in total)
Functional Keywordstranscription initiation, dna loading, transcription bubble, sigma factor, transcription
Biological sourceEscherichia coli (strain K12)
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Total number of polymer chains8
Total formula weight483181.50
Authors
Glyde, R.,Ye, F.Z.,Zhang, X.D. (deposition date: 2018-05-04, release date: 2018-07-04, Last modification date: 2024-05-15)
Primary citationGlyde, R.,Ye, F.,Jovanovic, M.,Kotta-Loizou, I.,Buck, M.,Zhang, X.
Structures of Bacterial RNA Polymerase Complexes Reveal the Mechanism of DNA Loading and Transcription Initiation.
Mol. Cell, 70:1111-1120.e3, 2018
Cited by
PubMed Abstract: Gene transcription is carried out by multi-subunit RNA polymerases (RNAPs). Transcription initiation is a dynamic multi-step process that involves the opening of the double-stranded DNA to form a transcription bubble and delivery of the template strand deep into the RNAP for RNA synthesis. Applying cryoelectron microscopy to a unique transcription system using σ (σ), the major bacterial variant sigma factor, we capture a new intermediate state at 4.1 Å where promoter DNA is caught at the entrance of the RNAP cleft. Combining with new structures of the open promoter complex and an initial de novo transcribing complex at 3.4 and 3.7 Å, respectively, our studies reveal the dynamics of DNA loading and mechanism of transcription bubble stabilization that involves coordinated, large-scale conformational changes of the universally conserved features within RNAP and DNA. In addition, our studies reveal a novel mechanism of strand separation by σ.
PubMed: 29932903
DOI: 10.1016/j.molcel.2018.05.021
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.1 Å)
Structure validation

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