Structural highlights
Publication Abstract from PubMed
The flavivirus NS5 harbors a methyltransferase (MTase) in its N-terminal approximately 265 residues and an RNA-dependent RNA polymerase (RdRP) within the C-terminal part. One of the major interests and challenges in NS5 is to understand the interplay between RdRP and MTase as a unique natural fusion protein in viral genome replication and cap formation. Here, we report the first crystal structure of the full-length flavivirus NS5 from Japanese encephalitis virus. The structure completes the vision for polymerase motifs F and G, and depicts defined intra-molecular interactions between RdRP and MTase. Key hydrophobic residues in the RdRP-MTase interface are highly conserved in flaviviruses, indicating the biological relevance of the observed conformation. Our work paves the way for further dissection of the inter-regulations of the essential enzymatic activities of NS5 and exploration of possible other conformations of NS5 under different circumstances.
Crystal Structure of the full-length Japanese encephalitis virus NS5 reveals a conserved methyltransferase-polymerase interface.,Lu G, Gong P PLoS Pathog. 2013;9(8):e1003549. doi: 10.1371/journal.ppat.1003549. Epub 2013 Aug, 8. PMID:23950717[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lu G, Gong P. Crystal Structure of the full-length Japanese encephalitis virus NS5 reveals a conserved methyltransferase-polymerase interface. PLoS Pathog. 2013;9(8):e1003549. doi: 10.1371/journal.ppat.1003549. Epub 2013 Aug, 8. PMID:23950717 doi:http://dx.doi.org/10.1371/journal.ppat.1003549
