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oligomer
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highly oligomeric at low salt concentrations
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x * 155000, SDS-PAGE
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x * 66000, calculated, x * 68000, SDS-PAGE
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x * 58200, about, sequence calculation
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x * 42000, recombinant His6-tagged NS5B, SDS-PAGE, x * 68000, recombinant RDRP, SDS-PAGE
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x * 82000, SDS-PAGE, fusion protein using the N-terminal domain of Escherichia coli lysyl-tRNA synthetase
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x * 103000, SDS-PAGE
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heterotrimer
composed of three subunits, PA, PB1 and PB2
heterotrimer
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the RNA polymerase complex consists of three subunits, PB1, PB2, and PA. These polymerase subunits and nucleoprotein, together with the viral RNA, form the viral ribonucleoprotein complex, which is the minimum component for viral RNA replication and transcription
heterotrimer
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the RNA polymerase of influenza virus is a heterotrimeric complex of PB1, PB2 and PA subunits, which cooperate in the transcription and replication of the viral genome. The N-terminal region of the PA subunit of two recent H5N1 strains can influence promoter binding
heterotrimer
the three subunits, PB1, PB2 and PA, are all required for both transcription and replication, PB1 carries the polymerase active site, PB2 includes the capped-RNA recognition domain, and PA, whose C-terminal domain consists of 13 alpha-helices and 9 beta-strands, is involved in assembly of the functional complex. The subunit interface is important for viral replication, overview
heterotrimer
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composed of three subunits, PA, PB1 and PB2
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monomer
1 * 60000, recombinant nontagged enzyme, SDS-PAGE
monomer
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monomers are observed at NaCl concentrations above 300 mM. Binding of short RNA substrates leads to a further increase in oligomerization, whereas GTP does not show any effect on protein/protein interactions. Nucleotide incorporation studies indicate the oligomerization state does not correlate with enzymatic activities
monomer
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1 * 128000, SDS-PAGE
tetramer
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the enzyme contains four nonidentical polypeptide chains, only one of which is a product of the phage genome. The other three subunits, present in uninfected cells are ribosomal protein S1 and protein synthesis elongation factors EF-Tu and EF-TS
tetramer
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x * 35000 + x * 450000 + x * 650000 + x * 700000, the enzyme is composed of 4 nonidentical subunits, only the 65000 Da subunit is phage-coded. The 70000 Da protein is 30S ribosomal protein S1 and the other two are the protein synthesis elongation factors Tu and Ts
tetramer
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composed of one phage-coded polypeptide and three host-supplied polypeptides
tetramer
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x * 35000 + x * 450000 + x * 650000 + x * 700000, the enzyme is composed of 4 nonidentical subunits, only the 65000 Da subunit is phage-coded. The 70000 Da protein is 30S ribosomal protein S1 and the other two are the protein synthesis elongation factors Tu and Ts
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tetramer
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the enzyme contains four nonidentical polypeptide chains, only one of which is a product of the phage genome. The other three subunits, present in uninfected cells are ribosomal protein S1 and protein synthesis elongation factors EF-Tu and EF-TS
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tetramer
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x * 35000 + x * 450000 + x * 650000 + x * 700000, the enzyme is composed of 4 nonidentical subunits, only the 65000 Da subunit is phage-coded. The 70000 Da protein is 30S ribosomal protein S1 and the other two are the protein synthesis elongation factors Tu and Ts
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trimer
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mechanism of nuclear import and assembly of the three polymerase subunits, PB1, PB2, and PA, overview. PB1 and PA form a dimer in the cytoplasm, which is imported into the nucleus separately from PB2. Once in the nucleus, the PB1/PA dimer associates with PB2 to form the trimeric polymerase. The strong interface that can be formed between the N-terminal extremity of PB2 and the C-terminal extremity of PB1 is present only in the fully assembled trimeric polymerase
trimer
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3 * 250000, the enzyme is a heterocomplex composed of one each of the three P-proteins: PB1, PB2 and PA. Each of them shows a MW of 250000 Da in glycerol gradient centrifugation
additional information
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the enzyme has a basic right-handed structure having a palm (residues 520-563, 641-735), thumb (residues 736-879) and fingers (residues 350-519, 564-640) subdomains. The central polymerase domain (PD) shows nucleotide binding properties, but neither the N-terminal domain (NTD) nor the C-terminal domain (CTD). Isolated PD does not exhibit RdRp activity but this activity can be reconstituted when all three domains are included in the reaction mixture. Molecular dynamics simulation suggests that the isolated PD has increased internal motions in comparison to when it is associated with the NTD and CTD. The motions of the separated PD may lead to the formation of a less accessible RNA template-binding channel and, thus, impair RdRp activity
additional information
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evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
Q8H1K9
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
Q9LKP0
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
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the nonstructural viral protein P1 is a component of the RdRp complex. The P1 protein is associated with at least six proteins in the infected cell
additional information
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evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
Cystovirus phi6
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structure-function analysis, molecular mapping, overview
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
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the enzyme contains four different subunits: I, II, II and IV. The molecular weights of which are 74000 Da, 60000 Da, 47000 Da and 36000 Da, respectively. Three of them, I, III and IV are host-coded proteins, ribosomal protein S1 and elongation factor Tu(III) and Ts(IV)
additional information
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open and closed enzyme conformation, and enzyme domain structure, structure-function relationship, overview
additional information
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structure of the RNA polymerase of poliovirus (1RA6) with subdomains fingers, palm, and thumb. Molecular dynamics simulations
additional information
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Qbeta replicase is composed of the bacteriophage Qbeta catalytic beta-subunit as well as the Escherichia coli host translation elongation factors EF-Tu and EF-Ts
additional information
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enzyme domain structure, structure-function relationship, overview
additional information
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enzyme domain structure, structure-function relationship, overview
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additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
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the enzyme is part, as RdRp_2 domain, of a 253-kDa polyprotein that also contains a papain-like protease, a methyltransferase, AlkB and helicase domains, a 5.2-kDa hydrophobic protein, a 58.5-kDa heat shock 70 protein homologue, a 60-kDa protein, a 30-kDa coat protein, and a 23-kDa protein
additional information
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the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
additional information
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open and closed enzyme conformation, and enzyme domain structure, structure-function relationship, overview
additional information
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open and closed enzyme conformation, and enzyme domain structure, structure-function relationship, overview
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additional information
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the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
additional information
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open and closed enzyme conformation, and enzyme domain structure, structure-function relationship, overview
additional information
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open and closed enzyme conformation, and enzyme domain structure, structure-function relationship, overview
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additional information
open and closed enzyme conformation, and enzyme domain structure, structure-function relationship, overview
additional information
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polymerase FluPol is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase active site, whereas PB2 and PA/P3 contain, respectively, cap-binding and endonuclease domains required for transcription initiation by cap-snatching. The apo-enzyme in closed conformation forms a compact particle with PB1 at its centre, capped on one face by PB2 and clamped between the two globular domains of P3. The endonuclease domain of P3 and the domains within the carboxy-terminal two-thirds of PB2 are completely rearranged. The cap-binding site is occluded by PB2, resulting in a conformation that is incompatible with transcription initiation. Tremendous flexibility of the protein complex. Comparison of apo-FluPolC with promoter-bound FluPolA
additional information
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the RNA-dependent RNA polymerase of arenaviruses is an integral part of the L protein, a 200-kDa multifunctional and multidomain protein, structure and function of the Lassa virus RdRp domain, folding model of the domain, overview
additional information
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the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
additional information
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the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
additional information
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RNA-dependent RNA polymerase complex, which consists of L protein (250000 Da) and P proteins (80000 Da)
additional information
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evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
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the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
additional information
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enzyme domain structure, structure-function relationship, overview
additional information
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evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
Q8LTE0
Qbeta replicase is composed of the bacteriophage Qbeta catalytic beta-subunit as well as the Escherichia coli host translation elongation factors EF-Tu and EF-Ts
additional information
crystal structure of RHDV RdRp reveals that the enzyme adopts a shape that resembles a right hand, with domains corresponding to the fingers, palm and thumb
additional information
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crystal structure of RHDV RdRp reveals that the enzyme adopts a shape that resembles a right hand, with domains corresponding to the fingers, palm and thumb
additional information
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crystal structure of RHDV RdRp reveals that the enzyme adopts a shape that resembles a right hand, with domains corresponding to the fingers, palm and thumb
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additional information
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the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
additional information
the core polymerase in respiratory syncytial virus (RSV) is composed of two proteins, a 250 kDa polymerase subunit (L), which contains the RNA-dependent RNA polymerase, the polyribonucleotidyl transferase (PRNTase, capping), and the methyltransferase enzymatic domains essential for viral transcription and replication, and the 27 kDa phosphoprotein (P) accessory protein
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
a transition model from the nsp7-nsp8 hexadecameric primase complex to the nsp12-nsp7-nsp8 polymerase complex is proposed to provide clues for the understanding of the coronavirus transcription and replication machinery
additional information
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a transition model from the nsp7-nsp8 hexadecameric primase complex to the nsp12-nsp7-nsp8 polymerase complex is proposed to provide clues for the understanding of the coronavirus transcription and replication machinery
additional information
cryo-electron microscopy structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9 A resolution
additional information
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cryo-electron microscopy structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9 A resolution
additional information
cryo-electron microscopy structure of the SARS-CoV-2 RdRp in an active form that mimics the replicating enzyme. The structure comprises the viral proteins non-structural protein 12 (nsp12), nsp8 and nsp7, and more than two turns of RNA template-product duplex. The active-site cleft of nsp12 binds to the first turn of RNA and mediates RdRp activity with conserved residues. Two copies of nsp8 bind to opposite sides of the cleft and position the second turn of RNA. Long helical extensions in nsp8 protrude along exiting RNA, forming positively charged sliding poles
additional information
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cryo-electron microscopy structure of the SARS-CoV-2 RdRp in an active form that mimics the replicating enzyme. The structure comprises the viral proteins non-structural protein 12 (nsp12), nsp8 and nsp7, and more than two turns of RNA template-product duplex. The active-site cleft of nsp12 binds to the first turn of RNA and mediates RdRp activity with conserved residues. Two copies of nsp8 bind to opposite sides of the cleft and position the second turn of RNA. Long helical extensions in nsp8 protrude along exiting RNA, forming positively charged sliding poles
additional information
cryo-EM structure of SARS-CoV-2 nsp12-nsp7-nsp8 core polymerase complex. The structure of the SARS-CoV-2 nsp12-nsp7-nsp8 complex is determined at 3.7-A resolution. The SARSCoV-2 polymerase complex consists of the nsp12 catalytic subunit and nsp7-nsp8 cofactors
additional information
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cryo-EM structure of SARS-CoV-2 nsp12-nsp7-nsp8 core polymerase complex. The structure of the SARS-CoV-2 nsp12-nsp7-nsp8 complex is determined at 3.7-A resolution. The SARSCoV-2 polymerase complex consists of the nsp12 catalytic subunit and nsp7-nsp8 cofactors
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
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RdRp structure comparative analysis, overview