| Structural highlights
6rfl is a 16 chain structure with sequence from [1] and Vaccinia virus glv-1h68. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | MG, ZN |
| NonStd Res: | SEP |
| Gene: | GL194 (Vaccinia virus GLV-1h68), GL169 (Vaccinia virus GLV-1h68), GL125 (Vaccinia virus GLV-1h68), GL151 (Vaccinia virus GLV-1h68), GL205 (Vaccinia virus GLV-1h68), GL076 (Vaccinia virus GLV-1h68), GL123 (Vaccinia virus GLV-1h68), GL167 (Vaccinia virus GLV-1h68), GL147 (Vaccinia virus GLV-1h68), H4L, List098, LIVPclone14_110, VAC_DPP10_113, VAC_DPP11_113, VAC_DPP12_113, VAC_DPP13_113, VAC_DPP15_113, VAC_DPP16_113, VAC_DPP17_113, VAC_DPP19_113, VAC_DPP20_113, VAC_DPP21_113, VAC_DPP9_113, VACAC2_113, VACCL3_113, VACV_098, VACV_TT9_123 (Vaccinia virus GLV-1h68), GL107 (Vaccinia virus GLV-1h68), GL155 (Vaccinia virus GLV-1h68), GL135 (Vaccinia virus GLV-1h68), GL087 (Vaccinia virus GLV-1h68) |
| Activity: | DNA-directed RNA polymerase, with EC number 2.7.7.6 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[B9U1M4_9POXV] Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes.[PIRNR:PIRNR000743] [B9U1I0_9POXV] Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes.[PIRNR:PIRNR000744] [B9U1R2_9POXV] Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes.[PIRNR:PIRNR000746]
Publication Abstract from PubMed
Poxviruses encode a multisubunit DNA-dependent RNA polymerase (vRNAP) that carries out viral gene expression in the host cytoplasm. We report cryo-EM structures of core and complete vRNAP enzymes from Vaccinia virus at 2.8 A resolution. The vRNAP core enzyme resembles eukaryotic RNA polymerase II (Pol II) but also reveals many virus-specific features, including the transcription factor Rap94. The complete enzyme additionally contains the transcription factor VETF, the mRNA processing factors VTF/CE and NPH-I, the viral core protein E11, and host tRNA(Gln). This complex can carry out the entire early transcription cycle. The structures show that Rap94 partially resembles the Pol II initiation factor TFIIB, that the vRNAP subunit Rpo30 resembles the Pol II elongation factor TFIIS, and that NPH-I resembles chromatin remodeling enzymes. Together with the accompanying paper (Hillen et al., 2019), these results provide the basis for unraveling the mechanisms of poxvirus transcription and RNA processing.
Structural Basis of Poxvirus Transcription: Vaccinia RNA Polymerase Complexes.,Grimm C, Hillen HS, Bedenk K, Bartuli J, Neyer S, Zhang Q, Huttenhofer A, Erlacher M, Dienemann C, Schlosser A, Urlaub H, Bottcher B, Szalay AA, Cramer P, Fischer U Cell. 2019 Dec 12;179(7):1537-1550.e19. doi: 10.1016/j.cell.2019.11.024. PMID:31835032[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Grimm C, Hillen HS, Bedenk K, Bartuli J, Neyer S, Zhang Q, Huttenhofer A, Erlacher M, Dienemann C, Schlosser A, Urlaub H, Bottcher B, Szalay AA, Cramer P, Fischer U. Structural Basis of Poxvirus Transcription: Vaccinia RNA Polymerase Complexes. Cell. 2019 Dec 12;179(7):1537-1550.e19. doi: 10.1016/j.cell.2019.11.024. PMID:31835032 doi:https://dx.doi.org/10.1016/j.cell.2019.11.024
|
