2GTH
crystal structure of the wildtype MHV coronavirus non-structural protein nsp15
Summary for 2GTH
| Entry DOI | 10.2210/pdb2gth/pdb |
| Descriptor | Replicase polyprotein 1ab (2 entities in total) |
| Functional Keywords | mhv, nsp15, viral protein |
| Biological source | Murine hepatitis virus |
| Cellular location | Non-structural protein 3: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 4: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 6: Host membrane; Multi-pass membrane protein (Potential). Non-structural protein 7: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 8: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 9: Host cytoplasm, host perinuclear region (By similarity). Non-structural protein 10: Host cytoplasm, host perinuclear region (By similarity). Helicase: Host endoplasmic reticulum-Golgi intermediate compartment (Potential). Uridylate-specific endoribonuclease: Host cytoplasm, host perinuclear region (By similarity): P16342 |
| Total number of polymer chains | 1 |
| Total formula weight | 41697.20 |
| Authors | |
| Primary citation | Xu, X.,Zhai, Y.,Sun, F.,Lou, Z.,Su, D.,Xu, Y.,Zhang, R.,Joachimiak, A.,Zhang, X.C.,Bartlam, M.,Rao, Z. New Antiviral Target Revealed by the Hexameric Structure of Mouse Hepatitis Virus Nonstructural Protein nsp15 J.Virol., 80:7909-7917, 2006 Cited by PubMed Abstract: The unique coronavirus transcription/replication machinery comprised of multiple virus-encoded nonstructural proteins (nsp) plays a vital role during initial and intermediate phases of the viral life cycle. The crystal structure of mouse hepatitis virus strain A59 (MHV-A59) nsp15 is reported at 2.15-A resolution. nsp15 is an XendoU endoribonuclease and is the first one from this family to have its structure unveiled. The MHV-A59 nsp15 monomer structure has a novel protein fold. Two nsp15 trimers form a back-to-back hexamer that is believed to be the functional unit. The structure reveals the catalytic site including the highly conserved residues His262, His277, and Lys317, which is supported by mutagenesis analysis. Gel filtration and enzyme activity assays confirmed that the hexamer is the active form for nsp15 and demonstrate the specificity of nsp15 for uridylate. The high sequence conservation of nsp15 in coronaviruses, including that of severe acute respiratory syndrome, suggests that this protein may provide a new target for the design of antiviral therapeutics. PubMed: 16873248DOI: 10.1128/JVI.00525-06 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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