5Y6R
Crystal structure of CSFV NS5B
Summary for 5Y6R
| Entry DOI | 10.2210/pdb5y6r/pdb |
| Descriptor | Genome polyprotein, SULFATE ION, GLYCEROL (3 entities in total) |
| Functional Keywords | virus, rdrp, polymerase, csfv, crystal, transferase |
| Biological source | Classical swine fever virus strain Eystrup |
| Total number of polymer chains | 1 |
| Total formula weight | 82836.31 |
| Authors | |
| Primary citation | Li, W.,Wu, B.,Soca, W.A.,An, L. Crystal Structure of Classical Swine Fever Virus NS5B Reveals a Novel N-Terminal Domain J. Virol., 92:-, 2018 Cited by PubMed Abstract: Classical swine fever virus (CSFV) is the cause of classical swine fever (CSF). Nonstructural protein 5B (NS5B) is an RNA-dependent RNA polymerase (RdRp) that is a key enzyme initiating viral RNA replication by a mechanism. It is also an attractive target for the development of anti-CSFV drugs. To gain a better understanding of the mechanism of CSFV RNA synthesis, here, we solved the first crystal structure of CSFV NS5B. Our studies show that the CSFV NS5B RdRp contains the characteristic finger, palm, and thumb domains, as well as a unique N-terminal domain (NTD) that has never been observed. Mutagenesis studies on NS5B validated the importance of the NTD in the catalytic activity of this novel RNA-dependent RNA polymerase. Moreover, our results shed light on CSFV infection. Pigs are important domesticated animals. However, a highly contagious viral disease named classical swine fever (CSF) causes devastating economic losses. Classical swine fever virus (CSFV), the primary cause of CSF, is a positive-sense single-stranded RNA virus belonging to the genus , family Genome replication of CSFV depends on an RNA-dependent RNA polymerase (RdRp) known as NS5B. However, the structure of CSFV NS5B has never been reported, and the mechanism of CSFV replication is poorly understood. Here, we solve the first crystal structure of CSFV NS5B and analyze the functions of the characteristic finger, palm, and thumb domains. Additionally, our structure revealed the presence of a novel N-terminal domain (NTD). Biochemical studies demonstrated that the NTD of CSFV NS5B is very important for RdRp activity. Collectively, our studies provide a structural basis for future rational design of anti-CSFV drugs, which is critically important, as no effective anti-CSFV drugs have been developed. PubMed: 29720518DOI: 10.1128/JVI.00324-18 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.01 Å) |
Structure validation
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