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7OQ4

Cryo-EM structure of the ATV RNAP Inhibitory Protein (RIP) bound to the DNA-binding channel of the host's RNA polymerase

Summary for 7OQ4
Entry DOI10.2210/pdb7oq4/pdb
Related7OK0
EMDB information13026
DescriptorDNA-directed RNA polymerase subunit A', DNA-directed RNA polymerase subunit L, DNA-directed RNA polymerase subunit N, ... (17 entities in total)
Functional Keywordsviral inhibitor, transcription inhibition, atv, archaeal virus, archaea, viral protein
Biological sourceAcidianus two-tailed virus (ATV)
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Total number of polymer chains14
Total formula weight423295.85
Authors
Pilotto, S.,Fouqueau, T.,Lukoyanova, N.,Sheppard, C.,Lucas-Staat, S.,Diaz-Santin, L.M.,Matelska, D.,Prangishvili, D.,Cheung, A.C.M.,Werner, F. (deposition date: 2021-06-02, release date: 2021-08-25, Last modification date: 2025-10-01)
Primary citationPilotto, S.,Fouqueau, T.,Lukoyanova, N.,Sheppard, C.,Lucas-Staat, S.,Diaz-Santin, L.M.,Matelska, D.,Prangishvili, D.,Cheung, A.C.M.,Werner, F.
Structural basis of RNA polymerase inhibition by viral and host factors.
Nat Commun, 12:5523-5523, 2021
Cited by
PubMed Abstract: RNA polymerase inhibition plays an important role in the regulation of transcription in response to environmental changes and in the virus-host relationship. Here we present the high-resolution structures of two such RNAP-inhibitor complexes that provide the structural bases underlying RNAP inhibition in archaea. The Acidianus two-tailed virus encodes the RIP factor that binds inside the DNA-binding channel of RNAP, inhibiting transcription by occlusion of binding sites for nucleic acid and the transcription initiation factor TFB. Infection with the Sulfolobus Turreted Icosahedral Virus induces the expression of the host factor TFS4, which binds in the RNAP funnel similarly to eukaryotic transcript cleavage factors. However, TFS4 allosterically induces a widening of the DNA-binding channel which disrupts trigger loop and bridge helix motifs. Importantly, the conformational changes induced by TFS4 are closely related to inactivated states of RNAP in other domains of life indicating a deep evolutionary conservation of allosteric RNAP inhibition.
PubMed: 34535646
DOI: 10.1038/s41467-021-25666-5
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.27 Å)
Structure validation

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数据于2025-10-15公开中

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