4K6M

Crystal Structure of the full-length Japanese encephalitis virus NS5

Summary for 4K6M

• Entry DOI: 10.2210/pdb4k6m/pdb
• Descriptor: Polyprotein, S-ADENOSYL-L-HOMOCYSTEINE, SULFATE ION, ... (5 entities in total)
• Functional Keywords: methyltransferase, rna-dependent rna polymerase, transferase
• Biological source: Japanese encephalitis virus
• Cellular location: Virion membrane; Multi-pass membrane protein: Q5NT71
• Total number of polymer chains: 2
• Total formula weight: 212102.39

Authors

Lu, G.,Gong, P. (deposition date: 2013-04-16, release date: 2013-08-28, Last modification date: 2023-11-08)

Primary citation

Lu, G.,Gong, P.
Crystal Structure of the full-length Japanese encephalitis virus NS5 reveals a conserved methyltransferase-polymerase interface
Plos Pathog., 9:e1003549-e1003549, 2013

PubMed Abstract: The flavivirus NS5 harbors a methyltransferase (MTase) in its N-terminal ≈ 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.

PubMed: 23950717
DOI: 10.1371/journal.ppat.1003549

Experimental method

X-RAY DIFFRACTION (2.6 Å)