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TitleCryo-EM structure of the respiratory syncytial virus RNA polymerase.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 368, Year 2020
Publish dateJan 17, 2020
AuthorsDongdong Cao / Yunrong Gao / Claire Roesler / Samantha Rice / Paul D'Cunha / Lisa Zhuang / Julia Slack / Mason Domke / Anna Antonova / Sarah Romanelli / Shayon Keating / Gabriela Forero / Puneet Juneja / Bo Liang /
PubMed AbstractThe respiratory syncytial virus (RSV) RNA polymerase, constituted of a 250 kDa large (L) protein and tetrameric phosphoprotein (P), catalyzes three distinct enzymatic activities - nucleotide ...The respiratory syncytial virus (RSV) RNA polymerase, constituted of a 250 kDa large (L) protein and tetrameric phosphoprotein (P), catalyzes three distinct enzymatic activities - nucleotide polymerization, cap addition, and cap methylation. How RSV L and P coordinate these activities is poorly understood. Here, we present a 3.67 Å cryo-EM structure of the RSV polymerase (L:P) complex. The structure reveals that the RNA dependent RNA polymerase (RdRp) and capping (Cap) domains of L interact with the oligomerization domain (P) and C-terminal domain (P) of a tetramer of P. The density of the methyltransferase (MT) domain of L and the N-terminal domain of P (P) is missing. Further analysis and comparison with other RNA polymerases at different stages suggest the structure we obtained is likely to be at an elongation-compatible stage. Together, these data provide enriched insights into the interrelationship, the inhibitors, and the evolutionary implications of the RSV polymerase.
External linksNat Commun / PubMed:31953395 / PubMed Central
MethodsEM (single particle)
Resolution3.67 Å
Structure data

20754

6uen

EMDB-20754, PDB-6uen:
Cryo-EM structure of the respiratory syncytial virus RNA polymerase
Method: EM (single particle) / Resolution: 3.67 Å

Source
  • human respiratory syncytial virus
KeywordsVIRAL PROTEIN/Transferase / Viral protein complexes / VIRAL PROTEIN / VIRAL PROTEIN-Transferase complex

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