4ewc

Crystal Structure of the Infectious Salmon Anemia Virus Nucleoprotein

spinqualitylabelsall models 4ewc, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ewc is a 1 chain structure with sequence from Salmon isavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NCAP_ISAV8 Encapsidates the negative strand viral RNA, protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication (PubMed:15522447). Publication Abstract from PubMed 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. The crystal structure and RNA-binding of an orthomyxovirus nucleoprotein.,Zheng W, Olson J, Vakharia V, Tao YJ PLoS Pathog. 2013 Sep;9(9):e1003624. doi: 10.1371/journal.ppat.1003624. Epub 2013, Sep 12. PMID:24068932 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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