5U0B
Structure of full-length Zika virus NS5
Summary for 5U0B
| Entry DOI | 10.2210/pdb5u0b/pdb |
| Related | 5U0C |
| Descriptor | Genome polyprotein, S-ADENOSYL-L-HOMOCYSTEINE, ZINC ION, ... (4 entities in total) |
| Functional Keywords | viral rna polymerase, transferase |
| Biological source | Zika virus (strain Mr 766) (ZIKV) |
| Total number of polymer chains | 2 |
| Total formula weight | 207904.21 |
| Authors | |
| Primary citation | Zhao, B.,Yi, G.,Du, F.,Chuang, Y.C.,Vaughan, R.C.,Sankaran, B.,Kao, C.C.,Li, P. Structure and function of the Zika virus full-length NS5 protein. Nat Commun, 8:14762-14762, 2017 Cited by PubMed Abstract: The recent outbreak of Zika virus (ZIKV) has infected over 1 million people in over 30 countries. ZIKV replicates its RNA genome using virally encoded replication proteins. Nonstructural protein 5 (NS5) contains a methyltransferase for RNA capping and a polymerase for viral RNA synthesis. Here we report the crystal structures of full-length NS5 and its polymerase domain at 3.0 Å resolution. The NS5 structure has striking similarities to the NS5 protein of the related Japanese encephalitis virus. The methyltransferase contains in-line pockets for substrate binding and the active site. Key residues in the polymerase are located in similar positions to those of the initiation complex for the hepatitis C virus polymerase. The polymerase conformation is affected by the methyltransferase, which enables a more efficiently elongation of RNA synthesis in vitro. Overall, our results will contribute to future studies on ZIKV infection and the development of inhibitors of ZIKV replication. PubMed: 28345656DOI: 10.1038/ncomms14762 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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