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7ADC

Transcription termination intermediate complex 3 delta NusG

Summary for 7ADC
Entry DOI10.2210/pdb7adc/pdb
EMDB information11723
DescriptorTranscription termination factor Rho, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (14 entities in total)
Functional Keywordsrna polymerase, rho, transcription
Biological sourceEscherichia coli
More
Total number of polymer chains15
Total formula weight793396.90
Authors
Said, N.,Hilal, T.,Loll, B.,Wahl, C.M. (deposition date: 2020-09-14, release date: 2020-11-25, Last modification date: 2021-02-03)
Primary citationSaid, N.,Hilal, T.,Sunday, N.D.,Khatri, A.,Burger, J.,Mielke, T.,Belogurov, G.A.,Loll, B.,Sen, R.,Artsimovitch, I.,Wahl, M.C.
Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase rho.
Science, 371:-, 2021
Cited by
PubMed Abstract: Factor-dependent transcription termination mechanisms are poorly understood. We determined a series of cryo-electron microscopy structures portraying the hexameric adenosine triphosphatase (ATPase) ρ on a pathway to terminating NusA/NusG-modified elongation complexes. An open ρ ring contacts NusA, NusG, and multiple regions of RNA polymerase, trapping and locally unwinding proximal upstream DNA. NusA wedges into the ρ ring, initially sequestering RNA. Upon deflection of distal upstream DNA over the RNA polymerase zinc-binding domain, NusA rotates underneath one capping ρ subunit, which subsequently captures RNA. After detachment of NusG and clamp opening, RNA polymerase loses its grip on the RNA:DNA hybrid and is inactivated. Our structural and functional analyses suggest that ρ, and other termination factors across life, may use analogous strategies to allosterically trap transcription complexes in a moribund state.
PubMed: 33243850
DOI: 10.1126/science.abd1673
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4 Å)
Structure validation

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