8FWL
Crystal structure of Australian bat lyssavirus nucleoprotein in complex with phosphoprotein chaperone
Summary for 8FWL
| Entry DOI | 10.2210/pdb8fwl/pdb |
| Descriptor | Phosphoprotein,Nucleoprotein, DI(HYDROXYETHYL)ETHER (3 entities in total) |
| Functional Keywords | chaperone, lyssavirus, nucleoprotein, phosphoprotein, rabies, viral protein |
| Biological source | Lyssavirus australis More |
| Total number of polymer chains | 1 |
| Total formula weight | 63901.60 |
| Authors | Donnelly, C.M.,Stewart, M.,Forwood, J.K. (deposition date: 2023-01-23, release date: 2023-03-08, Last modification date: 2024-03-20) |
| Primary citation | Donnelly, C.M.,Stewart, M.,Roby, J.A.,Sundaramoorthy, V.,Forwood, J.K. Structural Determination of the Australian Bat Lyssavirus Nucleoprotein and Phosphoprotein Complex. Viruses, 16:33-33, 2023 Cited by PubMed Abstract: Australian bat lyssavirus (ABLV) shows similar clinical symptoms as rabies, but there are currently no protein structures available for ABLV proteins. In lyssaviruses, the interaction between nucleoprotein (N) and phosphoprotein (N) in the absence of RNA generates a complex (NP) that is crucial for viral assembly, and understanding the interface between these two proteins has the potential to provide insight into a key feature: the viral lifecycle. In this study, we used recombinant chimeric protein expression and X-ray crystallography to determine the structure of ABLV nucleoprotein bound to residues 1-40 of its phosphoprotein chaperone. Comparison of our results with the recently generated structure of RABV CVS-11 NP demonstrated a highly conserved interface in this complex. Because the NP interface is conserved in the lyssaviruses of phylogroup I, it is an attractive therapeutic target for multiple rabies-causing viral species. PubMed: 38229694DOI: 10.3390/v16010033 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.19 Å) |
Structure validation
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