Key result
Structural analysis of the rotavirus VP1 RNA-dependent RNA polymerase revealed that active transcription induces conformational rearrangements in both VP1 and the DLP capsid shell protein.
Population
Intact virions, non-transcribing DLPs, and transcribing DLPs
Comparison
Transcribing DLPs vs non-transcribing DLPs and intact virions
Design
In situ structural analysis by local reconstruction of density around 5-fold positions
Authors
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Reveals rotavirus polymerase dynamics in situ; extends structural models but leaves open therapeutic translation.
The study provides a high-resolution in situ structure of the rotavirus VP1 RNA-dependent RNA polymerase, revealing conformational changes required for RNA transcription and exit.
Jenni et al. (2019) studied Rotavirus. Structural analysis of Rotavirus VP1 RdRp was evaluated on High-resolution structure of rotavirus VP1 RdRp in situ. Structural analysis of the rotavirus VP1 RNA-dependent RNA polymerase revealed that active transcription induces conformational rearrangements in both VP1 and the DLP capsid shell protein.
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