8QDJ
Ntaya virus methyltransferase in complex wih Sinefungin
Summary for 8QDJ
| Entry DOI | 10.2210/pdb8qdj/pdb |
| Descriptor | Ntaya virus methyltransferase, SINEFUNGIN, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | flavivirus, ntaya virus, sinefungin, methyltransferase, viral protein |
| Biological source | Ntaya virus |
| Total number of polymer chains | 1 |
| Total formula weight | 30045.39 |
| Authors | |
| Primary citation | Krejcova, K.,Krafcikova, P.,Klima, M.,Chalupska, D.,Chalupsky, K.,Zilecka, E.,Boura, E. Structural and functional insights in flavivirus NS5 proteins gained by the structure of Ntaya virus polymerase and methyltransferase. Structure, 32:1099-1109.e3, 2024 Cited by PubMed Abstract: Flaviviruses are single-stranded positive-sense RNA (+RNA) viruses that are responsible for several (re)emerging diseases such as yellow, dengue, or West Nile fevers. The Zika epidemic highlighted their dangerousness when a relatively benign virus known since the 1950s turned into a deadly pathogen. The central protein for their replication is NS5 (non-structural protein 5), which is composed of the N-terminal methyltransferase (MTase) domain and the C-terminal RNA-dependent RNA-polymerase (RdRp) domain. It is responsible for both RNA replication and installation of the 5' RNA cap. We structurally and biochemically analyzed the Ntaya virus MTase and RdRp domains and we compared their properties to other flaviviral NS5s. The enzymatic centers are well conserved across Flaviviridae, suggesting that the development of drugs targeting all flaviviruses is feasible. However, the enzymatic activities of the isolated proteins were significantly different for the MTase domains. PubMed: 38781970DOI: 10.1016/j.str.2024.04.020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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