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6UU6

E. coli sigma-S transcription initiation complex with a 4-nt RNA and a UTP ("Old" crystal soaked with UTP, ddCTP, and dinucleotide ApG for 30 minutes)

This is a non-PDB format compatible entry.
Summary for 6UU6
Entry DOI10.2210/pdb6uu6/pdb
DescriptorDNA-directed RNA polymerase subunit alpha, ZINC ION, MAGNESIUM ION, ... (11 entities in total)
Functional Keywordstranscription initiation, rna polymerase, dna promoter, transcription bubble, de novo rna synthesis, dna scrunching, sigma-s factor, transcription, transferase-dna-rna complex, transferase/dna/rna
Biological sourceEscherichia coli
More
Total number of polymer chains9
Total formula weight441631.91
Authors
Zuo, Y.,De, S.,Steitz, T.A. (deposition date: 2019-10-30, release date: 2020-08-26, Last modification date: 2024-11-20)
Primary citationZuo, Y.,De, S.,Feng, Y.,Steitz, T.A.
Structural Insights into Transcription Initiation from De Novo RNA Synthesis to Transitioning into Elongation.
Iscience, 23:101445-101445, 2020
Cited by
PubMed Abstract: In bacteria, the dissociable σ subunit of the RNA polymerase (RNAP) is responsible for initiating RNA synthesis from specific DNA sites. As nascent RNA grows, downstream DNA unwinds and is pulled into the RNAP, causing stress accumulation and initiation complex destabilization. Processive transcription elongation requires at least partial separation of the σ factor from the RNAP core enzyme. Here, we present a series of transcription complexes captured between the early initiation and elongation phases via in-crystal RNA synthesis and cleavage. Crystal structures of these complexes indicate that stress accumulation during transcription initiation is not due to clashing of the growing nascent RNA with the σ loop, but results from scrunching of the template strand DNA that is contained inside the RNAP by the σ domain. Our results shed light on how scrunching of template-strand DNA drives both abortive initiation and σ-RNAP core separation to transition transcription from initiation to elongation.
PubMed: 32829286
DOI: 10.1016/j.isci.2020.101445
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.201 Å)
Structure validation

230083

건을2025-01-15부터공개중

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