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Literature summary for 2.7.7.48 extracted from

  • Jenni, S.; Salgado, E.N.; Herrmann, T.; Li, Z.; Grant, T.; Grigorieff, N.; Trapani, S.; Estrozi, L.F.; Harrison, S.C.
    In situ structure of rotavirus VP1 RNA-dependent RNA polymerase (2019), J. Mol. Biol., 431, 3124-3138 .
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Rotavirus A A0A4Y1S1K6 Rotavirus cell entry results in loss of an outer protein layer and delivery into the cytosol of an intact, inner capsid particle (the double-layer particle or DLP). The RNA-dependent RNA polymerase (RdRp, VP1) is active inside the DLP. Each VP1 achieves many rounds of mRNA transcription from its associated genome segment. One VP1 molecule lies close to each fivefold axis of the icosahedrally symmetric DLP, just beneath the inner surface of its protein shell, embedded in tightly packed RNA. Outer layer dissociation enables the DLP to synthesize RNA, in vitro as well as in vivo, but appears not to induce any detectable structural change in the RdRp. Addition of NTPs, Mg2+, and S-adenosyl methionine, which allows active transcription, results in conformational rearrangements, in both VP1 and the DLP capsid shell protein, that allow a transcript to exit the polymerase and the particle. The position of VP1 (among the five symmetrically related alternatives) at one vertex does not correlate with its position at other vertices. This stochastic distribution of site occupancies limits long-range order in the 11-segment, dsRNA genome
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Rotavirus A RRV A0A4Y1S1K6 Rotavirus cell entry results in loss of an outer protein layer and delivery into the cytosol of an intact, inner capsid particle (the double-layer particle or DLP). The RNA-dependent RNA polymerase (RdRp, VP1) is active inside the DLP. Each VP1 achieves many rounds of mRNA transcription from its associated genome segment. One VP1 molecule lies close to each fivefold axis of the icosahedrally symmetric DLP, just beneath the inner surface of its protein shell, embedded in tightly packed RNA. Outer layer dissociation enables the DLP to synthesize RNA, in vitro as well as in vivo, but appears not to induce any detectable structural change in the RdRp. Addition of NTPs, Mg2+, and S-adenosyl methionine, which allows active transcription, results in conformational rearrangements, in both VP1 and the DLP capsid shell protein, that allow a transcript to exit the polymerase and the particle. The position of VP1 (among the five symmetrically related alternatives) at one vertex does not correlate with its position at other vertices. This stochastic distribution of site occupancies limits long-range order in the 11-segment, dsRNA genome
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Synonyms

Synonyms Comment Organism
RDRP
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Rotavirus A
RNA-dependent RNA polymerase
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Rotavirus A
VP1
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Rotavirus A