5KQS
Structure of NS5 methyltransferase from Zika virus bound to S-adenosylmethionine and 7-methyl-guanosine-5'-diphosphate
Summary for 5KQS
| Entry DOI | 10.2210/pdb5kqs/pdb |
| Related | 5KQR |
| Descriptor | Methyltransferase, 7N-METHYL-8-HYDROGUANOSINE-5'-DIPHOSPHATE, GLYCEROL, ... (7 entities in total) |
| Functional Keywords | zika, flavivirus, methyltransferase, ns5, transferase |
| Biological source | Zika virus (strain Mr 766) (ZIKV) |
| Cellular location | Virion membrane ; Multi-pass membrane protein : H9A910 |
| Total number of polymer chains | 1 |
| Total formula weight | 30918.81 |
| Authors | Coloma, J.,Jain, R.,Rajashankar, K.R.,Aggarwal, A.K. (deposition date: 2016-07-06, release date: 2016-09-14, Last modification date: 2023-10-04) |
| Primary citation | Coloma, J.,Jain, R.,Rajashankar, K.R.,Garcia-Sastre, A.,Aggarwal, A.K. Structures of NS5 Methyltransferase from Zika Virus. Cell Rep, 16:3097-3102, 2016 Cited by PubMed Abstract: The Zika virus (ZIKV) poses a major public health emergency. To aid in the development of antivirals, we present two high-resolution crystal structures of the ZIKV NS5 methyltransferase: one bound to S-adenosylmethionine (SAM) and the other bound to SAM and 7-methyl guanosine diphosphate (7-MeGpp). We identify features of ZIKV NS5 methyltransferase that lend to structure-based antiviral drug discovery. Specifically, SAM analogs with functionalities on the Cβ atom of the methionine portion of the molecules that occupy the RNA binding tunnel may provide better specificity relative to human RNA methyltransferases. PubMed: 27633330DOI: 10.1016/j.celrep.2016.08.091 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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