8BJW
Structure of Tupaia Paramyxovirus C protein
Summary for 8BJW
| Entry DOI | 10.2210/pdb8bjw/pdb |
| Descriptor | Protein C, DI(HYDROXYETHYL)ETHER (3 entities in total) |
| Functional Keywords | paramyxovirus non-structural protein c, viral protein |
| Biological source | Tupaia paramyxovirus |
| Total number of polymer chains | 6 |
| Total formula weight | 72242.43 |
| Authors | |
| Primary citation | Roy, A.,Chan Mine, E.,Gaifas, L.,Leyrat, C.,Volchkova, V.A.,Baudin, F.,Martinez-Gil, L.,Volchkov, V.E.,Karlin, D.G.,Bourhis, J.M.,Jamin, M. Orthoparamyxovirinae C Proteins Have a Common Origin and a Common Structural Organization. Biomolecules, 13:-, 2023 Cited by PubMed Abstract: The protein C is a small viral protein encoded in an overlapping frame of the P gene in the subfamily Orthoparamyxovirinae. This protein, expressed by alternative translation initiation, is a virulence factor that regulates viral transcription, replication, and production of defective interfering RNA, interferes with the host-cell innate immunity systems and supports the assembly of viral particles and budding. We expressed and purified full-length and an N-terminally truncated C protein from Tupaia paramyxovirus (TupV) C protein (genus Narmovirus). We solved the crystal structure of the C-terminal part of TupV C protein at a resolution of 2.4 Å and found that it is structurally similar to Sendai virus C protein, suggesting that despite undetectable sequence conservation, these proteins are homologous. We characterized both truncated and full-length proteins by SEC-MALLS and SEC-SAXS and described their solution structures by ensemble models. We established a mini-replicon assay for the related Nipah virus (NiV) and showed that TupV C inhibited the expression of NiV minigenome in a concentration-dependent manner as efficiently as the NiV C protein. A previous study found that the Orthoparamyxovirinae C proteins form two clusters without detectable sequence similarity, raising the question of whether they were homologous or instead had originated independently. Since TupV C and SeV C are representatives of these two clusters, our discovery that they have a similar structure indicates that all Orthoparamyxovirine C proteins are homologous. Our results also imply that, strikingly, a STAT1-binding site is encoded by exactly the same RNA region of the P/C gene across Paramyxovirinae, but in different reading frames (P or C), depending on which cluster they belong to. PubMed: 36979390DOI: 10.3390/biom13030455 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.39 Å) |
Structure validation
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