6RIC
Structure of the core Vaccinia Virus DNA-dependent RNA polymerase complex
Summary for 6RIC
| Entry DOI | 10.2210/pdb6ric/pdb |
| Related | 6RFL 6RID 6RIE |
| EMDB information | 4868 4888 |
| Descriptor | DNA-dependent RNA polymerase subunit rpo147, MAGNESIUM ION, ZINC ION, ... (11 entities in total) |
| Functional Keywords | vaccinia, rna polymerase, transcription, gene expression, viral protein |
| Biological source | Vaccinia virus GLV-1h68 More |
| Total number of polymer chains | 9 |
| Total formula weight | 505343.91 |
| Authors | Grimm, C.,Hillen, H.S.,Bedenk, K.,Bartuli, J.,Neyer, S.,Zhang, Q.,Huettenhofer, A.,Erlacher, M.,Dienemann, C.,Schlosser, A.,Urlaub, H.,Boettcher, B.,Szalay, A.,Cramer, P.,Fischer, U. (deposition date: 2019-04-23, release date: 2019-12-18, Last modification date: 2025-12-17) |
| Primary citation | Hillen, H.S.,Bartuli, J.,Grimm, C.,Dienemann, C.,Bedenk, K.,Szalay, A.A.,Fischer, U.,Cramer, P. Structural Basis of Poxvirus Transcription: Transcribing and Capping Vaccinia Complexes. Cell, 179:1525-, 2019 Cited by PubMed Abstract: Poxviruses use virus-encoded multisubunit RNA polymerases (vRNAPs) and RNA-processing factors to generate mG-capped mRNAs in the host cytoplasm. In the accompanying paper, we report structures of core and complete vRNAP complexes of the prototypic Vaccinia poxvirus (Grimm et al., 2019; in this issue of Cell). Here, we present the cryo-electron microscopy (cryo-EM) structures of Vaccinia vRNAP in the form of a transcribing elongation complex and in the form of a co-transcriptional capping complex that contains the viral capping enzyme (CE). The trifunctional CE forms two mobile modules that bind the polymerase surface around the RNA exit tunnel. RNA extends from the vRNAP active site through this tunnel and into the active site of the CE triphosphatase. Structural comparisons suggest that growing RNA triggers large-scale rearrangements on the surface of the transcription machinery during the transition from transcription initiation to RNA capping and elongation. Our structures unravel the basis for synthesis and co-transcriptional modification of poxvirus RNA. PubMed: 31835031DOI: 10.1016/j.cell.2019.11.023 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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