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Literature summary extracted from

  • Hengrung, N.; El Omari, K.; Serna Martin, I.; Vreede, F.T.; Cusack, S.; Rambo, R.P.; Vonrhein, C.; Bricogne, G.; Stuart, D.I.; Grimes, J.M.; Fodor, E.
    Crystal structure of the RNA-dependent RNA polymerase from influenza C virus (2015), Nature, 527, 114-117.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.48 purified apo-FluPol in closed conformation, sitting-drop vapour-diffusion, protein:precipitant ratio of 2:1, mixing of 5 mg/ml protein with either 70% v/v Morpheus G2, supplemented with 0%-1% 1 M NaOH, to generate P43212 crystals, or with crystal-seeds and 0.2 M NaCl, 0.1 M Na-HEPES, pH 7.5, and 25% w/v PEG 4000 for P212121 crystals, 20°C, heavy atom derivatization by P43212 crystals soaking in a solution of gold(I) potassium cyanide dissolved in mother liquor, for 2-3 h at 20°C, X-ray diffraction structure determination and analysis at 3.9 A resolution influenza C virus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.48 nucleoside triphosphate + RNAn influenza C virus
-
 diphosphate + RNAn+1
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.48 influenza C virus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.48 nucleoside triphosphate + RNAn
-
 influenza C virus diphosphate + RNAn+1
-
 ?
2.7.7.48 nucleoside triphosphate + RNAn replication occurs through de novo initiation and involves a complementary RNA intermediate influenza C virus diphosphate + RNAn+1
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.7.48 More 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 influenza C virus

Synonyms

EC Number Synonyms Comment Organism
2.7.7.48 FluPol
-
 influenza C virus

General Information

EC Number General Information Comment Organism
2.7.7.48 additional information 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. Comparison of apo-FluPolC with promoter-bound FluPolA, overview influenza C virus
2.7.7.48 physiological function negative-sense RNA viruses, such as influenza, encode large, multidomain RNA-dependent RNA polymerases that can both transcribe and replicate the viral RNA genome. Replication occurs through de novo initiation and involves a complementary RNA intermediate influenza C virus