5XJ0

T. thermophilus RNA polymerase holoenzyme bound with gp39 and gp76

5XJ0 の概要

• エントリーDOI: 10.2210/pdb5xj0/pdb
• 関連するPDBエントリー: 3WOD
• 分子名称: DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (8 entities in total)
• 機能のキーワード: transcription regulation by bacteriophage-encoded proteins, transferase-transcription complex, transferase/transcription
• 由来する生物種: Thermus virus P23-45; 詳細
• 細胞内の位置: Cytoplasm : Q5SKW1
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 465889.38

構造登録者

Ooi, W.Y.,Murayama, Y.,Mekler, V.,Minakhin, L.,Severinov, K.,Yokoyama, S.,Sekine, S. (登録日: 2017-04-28, 公開日: 2017-12-20, 最終更新日: 2023-11-22)

主引用文献

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
Nucleic Acids Res., 46:431-441, 2018

PubMed Abstract: RNA polymerase (RNAP) is a major target of gene regulation. Thermus thermophilus bacteriophage P23-45 encodes two RNAP binding proteins, gp39 and gp76, which shut off host gene transcription while allowing orderly transcription of phage genes. We previously reported the structure of the T. thermophilus RNAP•σA holoenzyme complexed with gp39. Here, we solved the structure of the RNAP•σA holoenzyme bound with both gp39 and gp76, which revealed an unprecedented inhibition mechanism by gp76. The acidic protein gp76 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 T. thermophilus RNAP from most host promoters. gp76 is less inhibitory for phage transcription, as tighter RNAP interaction with the phage promoters allows the template DNA to compete with gp76 for the common binding site. gp76 also inhibits Escherichia coli RNAP highlighting the template-DNA binding site as a new target site for developing antibacterial agents.

PubMed: 29165680
DOI: 10.1093/nar/gkx1162

実験手法

X-RAY DIFFRACTION (4.004 Å)