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8URB

Porcine epidemic diarrhea virus complete core polymerase complex

Summary for 8URB
Entry DOI10.2210/pdb8urb/pdb
Related8G6R
EMDB information42488
Descriptornsp12, nsp8, nsp7, ... (6 entities in total)
Functional Keywordscoronavirus, nsp12, rna polymerase, pedv, replication, transferase-rna complex, transferase/rna
Biological sourcePorcine epidemic diarrhea virus
More
Total number of polymer chains6
Total formula weight189998.60
Authors
Anderson, T.K.,Kirchdoerfer, R.N. (deposition date: 2023-10-25, release date: 2023-11-15)
Primary citationAnderson, T.K.,Hoferle, P.J.,Lee, K.W.,Coon, J.J.,Kirchdoerfer, R.N.
An alphacoronavirus polymerase structure reveals conserved co-factor functions.
Biorxiv, 2023
Cited by
PubMed Abstract: Coronaviruses are a diverse subfamily of viruses containing pathogens of humans and animals. This subfamily of viruses replicates their RNA genomes using a core polymerase complex composed of viral non-structural proteins: nsp7, nsp8 and nsp12. Most of our understanding of coronavirus molecular biology comes from the betacoronaviruses like SARS-CoV and SARS-CoV-2, the latter of which is the causative agent of COVID-19. In contrast, members of the alphacoronavirus genus are relatively understudied despite their importance in human and animal health. Here we have used cryo-electron microscopy to determine the structure of the alphacoronavirus porcine epidemic diarrhea virus (PEDV) core polymerase complex bound to RNA. Our structure shows an unexpected nsp8 stoichiometry in comparison to other published coronavirus polymerase structures. Biochemical analysis shows that the N-terminal extension of one nsp8 is not required for RNA synthesis for alpha and betacoronaviruses as previously hypothesized. Our work shows the importance of studying diverse coronaviruses to reveal aspects of coronavirus replication while also identifying areas of conservation to be targeted by antiviral drugs.
PubMed: 36993498
DOI: 10.1101/2023.03.15.532841
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

227344

数据于2024-11-13公开中

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