1iw7
Crystal structure of the RNA polymerase holoenzyme from Thermus thermophilus at 2.6A resolution
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OverviewOverview
In bacteria, the binding of a single protein, the initiation factor sigma, to a multi-subunit RNA polymerase core enzyme results in the formation of, a holoenzyme, the active form of RNA polymerase essential for, transcription initiation. Here we report the crystal structure of a, bacterial RNA polymerase holoenzyme from Thermus thermophilus at 2.6 A, resolution. In the structure, two amino-terminal domains of the sigma, subunit form a V-shaped structure near the opening of the upstream, DNA-binding channel of the active site cleft. The carboxy-terminal domain, of sigma is near the outlet of the RNA-exit channel, about 57 A from the, N-terminal domains. The extended linker domain forms a hairpin protruding, into the active site cleft, then stretching through the RNA-exit channel, to connect the N- and C-terminal domains. The holoenzyme structure, provides insight into the structural organization of transcription, intermediate complexes and into the mechanism of transcription initiation.
About this StructureAbout this Structure
1IW7 is a Protein complex structure of sequences from Thermus thermophilus with PB and MG as ligands. The following page contains interesting information on the relation of 1IW7 with [Catabolite Activator Protein]. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution., Vassylyev DG, Sekine S, Laptenko O, Lee J, Vassylyeva MN, Borukhov S, Yokoyama S, Nature. 2002 Jun 13;417(6890):712-9. Epub 2002 May 8. PMID:12000971
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