2wfs

Fitting of influenza virus NP structure into the 9-fold symmetryzed cryoEM reconstruction of an active RNP particle.

spinqualitylabelsall models 2wfs, resolution 12.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wfs is a 9 chain structure with sequence from 9infa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: NP (9INFA) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed The influenza viruses contain a segmented, single-stranded RNA genome of negative polarity. Each RNA segment is encapsidated by the nucleoprotein and the polymerase complex into ribonucleoprotein particles (RNPs), which are responsible for virus transcription and replication. Despite their importance, information about the structure of these RNPs is scarce. We have determined the three-dimensional structure of a biologically active recombinant RNP by cryo-electron microscopy. The structure shows a nonameric nucleoprotein ring (at 12 Angstrom resolution) with two monomers connected to the polymerase complex (at 18 Angstrom resolution). Docking the atomic structures of the nucleoprotein and polymerase domains, as well as mutational analyses, has allowed us to define the interactions between the functional elements of the RNP and to propose the location of the viral RNA. Our results provide the first model for a functional negative-stranded RNA virus ribonucleoprotein complex. The structure reported here will serve as a framework to generate a quasi-atomic model of the molecular machine responsible for viral RNA synthesis and to test new models for virus RNA replication and transcription. The structure of a biologically active influenza virus ribonucleoprotein complex.,Coloma R, Valpuesta JM, Arranz R, Carrascosa JL, Ortin J, Martin-Benito J PLoS Pathog. 2009 Jun;5(6):e1000491. Epub 2009 Jun 26. PMID:19557158 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nucleoprotein

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