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6BJS

CryoEM structure of E.coli his pause elongation complex without pause hairpin

Summary for 6BJS
Entry DOI10.2210/pdb6bjs/pdb
EMDB information7002 7103
DescriptorDNA (32-MER), RNA (29-MER), DNA-directed RNA polymerase subunit alpha, ... (9 entities in total)
Functional Keywordsdna-dependent rna polymerase, transcription, paused elongation complex, transcription-dna-rna complex, transcription/dna/rna
Biological sourceEscherichia coli (strain K12)
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Total number of polymer chains8
Total formula weight398329.64
Authors
Kang, J.Y.,Landick, R.,Darst, S.A. (deposition date: 2017-11-06, release date: 2018-03-28, Last modification date: 2024-03-13)
Primary citationKang, J.Y.,Mishanina, T.V.,Bellecourt, M.J.,Mooney, R.A.,Darst, S.A.,Landick, R.
RNA Polymerase Accommodates a Pause RNA Hairpin by Global Conformational Rearrangements that Prolong Pausing.
Mol. Cell, 69:802-815.e1, 2018
Cited by
PubMed Abstract: Sequence-specific pausing by RNA polymerase (RNAP) during transcription plays crucial and diverse roles in gene expression. In bacteria, RNA structures are thought to fold within the RNA exit channel of the RNAP and can increase pause lifetimes significantly. The biophysical mechanism of pausing is uncertain. We used single-particle cryo-EM to determine structures of paused complexes, including a 3.8-Å structure of an RNA hairpin-stabilized, paused RNAP that coordinates RNA folding in the his operon attenuation control region of E. coli. The structures revealed a half-translocated pause state (RNA post-translocated, DNA pre-translocated) that can explain transcriptional pausing and a global conformational change of RNAP that allosterically inhibits trigger loop folding and can explain pause hairpin action. Pause hairpin interactions with the RNAP RNA exit channel suggest how RNAP guides the formation of nascent RNA structures.
PubMed: 29499135
DOI: 10.1016/j.molcel.2018.01.018
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (5.5 Å)
Structure validation

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