2WA1
Structure of the methyltransferase domain from Modoc Virus, a Flavivirus with No Known Vector (NKV)
Summary for 2WA1
| Entry DOI | 10.2210/pdb2wa1/pdb |
| Related | 2WA2 |
| Descriptor | NON-STRUCTURAL PROTEIN 5, SULFATE ION (3 entities in total) |
| Functional Keywords | transferase, transmembrane, envelope protein, virus replication, virion, membrane, flavivirus, modoc virus, 2'-o- methyltransferase, methyltransferase, n7-methyltransferase |
| Biological source | MODOC VIRUS |
| Cellular location | Envelope protein E: Virion membrane; Multi- pass membrane protein: Q8QL64 |
| Total number of polymer chains | 2 |
| Total formula weight | 61720.50 |
| Authors | Jansson, A.M.,Johansson, P.,Jones, T.A. (deposition date: 2009-02-02, release date: 2009-08-04, Last modification date: 2024-11-20) |
| Primary citation | Jansson, A.M.,Jakobsson, E.,Johansson, P.,Lantez, V.,Coutard, B.,De Lamballerie, X.,Unge, T.,Jones, T.A. Structure of the Methyltransferase Domain from the Modoc Virus, a Flavivirus with No Known Vector. Acta Crystallogr.,Sect.D, 65:796-, 2009 Cited by PubMed Abstract: The Modoc virus (MODV) is a flavivirus with no known vector (NKV). Evolutionary studies have shown that the viruses in the MODV group have evolved in association with mammals (bats, rodents) without transmission by an arthropod vector. MODV methyltransferase is the first enzyme from this evolutionary branch to be structurally characterized. The high-resolution structure of the methyltransferase domain of the MODV NS5 protein (MTase(MODV)) was determined. The protein structure was solved in the apo form and in complex with its cofactor S-adenosyl-L-methionine (SAM). Although it belongs to a separate evolutionary branch, MTase(MODV) shares structural characteristics with flaviviral MTases from the other branches. Its capping machinery is a relatively new target in flaviviral drug development and the observed structural conservation between the three flaviviral branches indicates that it may be possible to identify a drug that targets a range of flaviviruses. The structural conservation also supports the choice of MODV as a possible model for flavivirus studies. PubMed: 19622863DOI: 10.1107/S0907444909017260 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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