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Literature summary for 2.7.7.6 extracted from

  • Ooi, W.Y.; Murayama, Y.; Mekler, V.; Minakhin, L.; Severinov, K.; Yokoyama, S.; Sekine, S.I.
    A Thermus phage protein inhibits host RNA polymerase by preventing template DNA strand loading during open promoter complex formation (2018), Nucleic Acids Res., 46, 431-441 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.6

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapor diffusion technique, cocrystallization of the Thermus thermophilus RNAP holoenzyme and gp39 Thermus thermophilus

Inhibitors

Inhibitors Comment Organism Structure
protein gp76 the Thermus phage protein gp76 inhibits Escherichia coli RNAP highlighting the template-DNA binding site as a target site for developing antibacterial agents Escherichia coli
protein gp76 the Thermus phage protein binds within the RNAP cleft and occupies the path of the template DNA strand at positions -11 to -4, relative to the transcription start site at +1. Thus, gp76 obstructs the formation of an open promoter complex and prevents transcription by Thermus thermophilus RNAP from most host promoters Thermus thermophilus

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Thermus thermophilus Q5SHR6 AND Q8RQE9 AND Q8RQE8 AND Q8RQE7 Q5SHR6: subunit alpha, Q8RQE9: subunit beta, Q8RQE8: subunit beta', Q8RQE7: subunit omega
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Synonyms

Synonyms Comment Organism
RNAP
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 Escherichia coli
RNAP
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 Thermus thermophilus

General Information

General Information Comment Organism
drug target the template-DNA binding site is a target site for developing antibacterial agents Escherichia coli
drug target the template-DNA binding site is a target site for developing antibacterial agents Thermus thermophilus
additional information RNA polymerase is a major target of gene regulation Escherichia coli
additional information RNA polymerase is a major target of gene regulation Thermus thermophilus