4EWC
Crystal Structure of the Infectious Salmon Anemia Virus Nucleoprotein
Summary for 4EWC
Entry DOI | 10.2210/pdb4ewc/pdb |
Descriptor | Putative nucleoprotein (2 entities in total) |
Functional Keywords | alpha-helical, rna encapsidation, isavirus, orthomyoxovirus, nucleoprotein, np, rna binding, replication, transcription, viral rna packaging, rna binding protein |
Biological source | Infectious salmon anemia virus |
Total number of polymer chains | 1 |
Total formula weight | 68313.72 |
Authors | |
Primary citation | Zheng, W.,Olson, J.,Vakharia, V.,Tao, Y.J. The crystal structure and RNA-binding of an orthomyxovirus nucleoprotein. Plos Pathog., 9:e1003624-e1003624, 2013 Cited by PubMed Abstract: Genome packaging for viruses with segmented genomes is often a complex problem. This is particularly true for influenza viruses and other orthomyxoviruses, whose genome consists of multiple negative-sense RNAs encapsidated as ribonucleoprotein (RNP) complexes. To better understand the structural features of orthomyxovirus RNPs that allow them to be packaged, we determined the crystal structure of the nucleoprotein (NP) of a fish orthomyxovirus, the infectious salmon anemia virus (ISAV) (genus Isavirus). As the major protein component of the RNPs, ISAV-NP possesses a bi-lobular structure similar to the influenza virus NP. Because both RNA-free and RNA-bound ISAV NP forms stable dimers in solution, we were able to measure the NP RNA binding affinity as well as the stoichiometry using recombinant proteins and synthetic oligos. Our RNA binding analysis revealed that each ISAV-NP binds ~12 nts of RNA, shorter than the 24-28 nts originally estimated for the influenza A virus NP based on population average. The 12-nt stoichiometry was further confirmed by results from electron microscopy and dynamic light scattering. Considering that RNPs of ISAV and the influenza viruses have similar morphologies and dimensions, our findings suggest that NP-free RNA may exist on orthomyxovirus RNPs, and selective RNP packaging may be accomplished through direct RNA-RNA interactions. PubMed: 24068932DOI: 10.1371/journal.ppat.1003624 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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