5XJ0
T. thermophilus RNA polymerase holoenzyme bound with gp39 and gp76
Summary for 5XJ0
| Entry DOI | 10.2210/pdb5xj0/pdb |
| Related | 3WOD |
| Descriptor | DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (8 entities in total) |
| Functional Keywords | transcription regulation by bacteriophage-encoded proteins, transferase-transcription complex, transferase/transcription |
| Biological source | Thermus virus P23-45 More |
| Cellular location | Cytoplasm : Q5SKW1 |
| Total number of polymer chains | 9 |
| Total formula weight | 465889.38 |
| Authors | Ooi, W.Y.,Murayama, Y.,Mekler, V.,Minakhin, L.,Severinov, K.,Yokoyama, S.,Sekine, S. (deposition date: 2017-04-28, release date: 2017-12-20, Last modification date: 2023-11-22) |
| Primary citation | 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 Cited by 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: 29165680DOI: 10.1093/nar/gkx1162 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.004 Å) |
Structure validation
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