6ric | pdb_00006ric

Structure of the core Vaccinia Virus DNA-dependent RNA polymerase complex

spinqualitylabelsall models 6ric, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ric is a 9 chain structure with sequence from Vaccinia virus glv-1h68. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, ZN Related: 6rfl, 6rid, 6rie Gene: GL125 (Vaccinia virus GLV-1h68), GL194 (Vaccinia virus GLV-1h68), GL205 (Vaccinia virus GLV-1h68), GL123 (Vaccinia virus GLV-1h68), GL167 (Vaccinia virus GLV-1h68), GL147 (Vaccinia virus GLV-1h68), GL130 (Vaccinia virus GLV-1h68), GL107 (Vaccinia virus GLV-1h68), GL076 (Vaccinia virus GLV-1h68) Activity: DNA-directed RNA polymerase, with EC number 2.7.7.6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [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] [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] [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] Publication Abstract from PubMed Poxviruses use virus-encoded multisubunit RNA polymerases (vRNAPs) and RNA-processing factors to generate m(7)G-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. Structural Basis of Poxvirus Transcription: Transcribing and Capping Vaccinia Complexes.,Hillen HS, Bartuli J, Grimm C, Dienemann C, Bedenk K, Szalay AA, Fischer U, Cramer P Cell. 2019 Dec 12;179(7):1525-1536.e12. doi: 10.1016/j.cell.2019.11.023. PMID:31835031 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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