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Literature summary for 2.7.7.6 extracted from

  • Belogurov, G.A.; Vassylyeva, M.N.; Sevostyanova, A.; Appleman, J.R.; Xiang, A.X.; Lira, R.; Webber, S.E.; Klyuyev, S.; Nudler, E.; Artsimovitch, I.; Vassylyev, D.G.
    Transcription inactivation through local refolding of the RNA polymerase structure (2009), Nature, 457, 332-335.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.6

Inhibitors

Inhibitors Comment Organism Structure
myxopyronin inhibits bacterial RNA polymerase and inhibits transcription on the artificially melted promoters, inhibition mechanism, overview. The antibiotic binds to a pocket deep inside the RNAP clamp head domain, which interacts with the DNA template in the transcription bubble, binding of dMyx stabilizes refolding of the beta'-subunit switch-2 segment, resulting in a configuration that might indirectly compromise binding to, or directly clash with, the melted template DNA strand, binding structure, overview. Antibiotic binding does not prevent nucleation of the promoter DNA melting but instead blocks its propagation towards the active site. dMyx binds in the pocket deep inside the RNAP clamp head domain. Mutations designed in switch-2 mimic the dMyx effects on promoter complexes in the absence of antibiotic Thermus thermophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ bound at the active site Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the RNAP clamp head domain constitutes the wall of the main channel opposite the catalytic centre and forms crucial contacts with the DNA template strand in the elongation complex Thermus thermophilus ?
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 ?

Synonyms

Synonyms Comment Organism
RNA polymerase
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 Thermus thermophilus
RNAP
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 Thermus thermophilus