2HCS
Crystal structure of RNA dependant RNA polymerase domain of West Nile virus
Summary for 2HCS
| Entry DOI | 10.2210/pdb2hcs/pdb |
| Related | 2HCN |
| Descriptor | RNA-directed RNA polymerase (NS5), ZINC ION (3 entities in total) |
| Functional Keywords | west-nile virus rna polymerase, structural genomics, marseilles structural genomics program @ afmb, msgp, vizier, viral enzymes involved in replication, transferase |
| Biological source | Kunjin virus |
| Cellular location | Capsid protein C: Virion (Potential). Peptide pr: Secreted (By similarity). Small envelope protein M: Virion membrane; Multi-pass membrane protein (By similarity). Envelope protein E: Virion membrane; Multi- pass membrane protein (By similarity). Non-structural protein 1: Secreted. Non-structural protein 2A: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease subunit NS2B: Host endoplasmic reticulum membrane; Multi-pass membrane protein (Potential). Serine protease NS3: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity). Non-structural protein 4A: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). Non-structural protein 4B: Host endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity). RNA-directed RNA polymerase NS5: Host endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P14335 |
| Total number of polymer chains | 1 |
| Total formula weight | 68462.47 |
| Authors | Egloff, M.P.,Malet, H.,Marseilles Structural Genomics Program @ AFMB (MSGP) (deposition date: 2006-06-18, release date: 2007-02-06, Last modification date: 2024-02-14) |
| Primary citation | Malet, H.,Egloff, M.P.,Selisko, B.,Butcher, R.E.,Wright, P.J.,Roberts, M.,Gruez, A.,Sulzenbacher, G.,Vonrhein, C.,Bricogne, G.,Mackenzie, J.M.,Khromykh, A.A.,Davidson, A.D.,Canard, B. Crystal structure of the RNA polymerase domain of the West Nile virus non-structural protein 5 J.Biol.Chem., 282:10678-10689, 2007 Cited by PubMed Abstract: Viruses of the family Flaviviridae are important human and animal pathogens. Among them, the Flaviviruses dengue (DENV) and West Nile (WNV) cause regular outbreaks with fatal outcomes. The RNA-dependent RNA polymerase (RdRp) activity of the non-structural protein 5 (NS5) is a key activity for viral RNA replication. In this study, crystal structures of enzymatically active and inactive WNV RdRp domains were determined at 3.0- and 2.35-A resolution, respectively. The determined structures were shown to be mostly similar to the RdRps of the Flaviviridae members hepatitis C and bovine viral diarrhea virus, although with unique elements characteristic for the WNV RdRp. Using a reverse genetic system, residues involved in putative interactions between the RNA-cap methyltransferase (MTase) and the RdRp domain of Flavivirus NS5 were identified. This allowed us to propose a model for the structure of the full-length WNV NS5 by in silico docking of the WNV MTase domain (modeled from our previously determined structure of the DENV MTase domain) onto the RdRp domain. The Flavivirus RdRp domain structure determined here should facilitate both the design of anti-Flavivirus drugs and structure-function studies of the Flavivirus replication complex in which the multifunctional NS5 protein plays a central role. PubMed: 17287213DOI: 10.1074/jbc.M607273200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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