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Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.6 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

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

Organism

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

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.6 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

EC Number Synonyms Comment Organism
2.7.7.6 RNA polymerase
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Thermus thermophilus
2.7.7.6 RNAP
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Thermus thermophilus