5ooo | pdb_00005ooo

Structure of the Rift Valley fever virus NSs protein core domain

spinqualitylabelsall models 5ooo, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ooo is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Rift Valley fever phlebovirus (RVFV) is a clinically and economically important pathogen increasingly likely to cause widespread epidemics. RVFV virulence depends on the interferon antagonist non-structural protein (NSs), which remains poorly characterized. We identified a stable core domain of RVFV NSs (residues 83-248), and solved its crystal structure, a novel all-helical fold organized into highly ordered fibrils. A hallmark of RVFV pathology is NSs filament formation in infected cell nuclei. Recombinant virus encoding the NSs core domain induced intranuclear filaments, suggesting it contains all essential determinants for nuclear translocation and filament formation. Mutations of key crystal fibril interface residues in viruses encoding full-length NSs completely abrogated intranuclear filament formation in infected cells. We propose the fibrillar arrangement of the NSs core domain in crystals reveals the molecular basis of assembly of this key virulence factor in cell nuclei. Our findings have important implications for fundamental understanding of RVFV virulence. Rift Valley fever phlebovirus NSs protein core domain structure suggests molecular basis for nuclear filaments.,Barski M, Brennan B, Miller OK, Potter JA, Vijayakrishnan S, Bhella D, Naismith JH, Elliott RM, Schwarz-Linek U Elife. 2017 Sep 15;6. pii: e29236. doi: 10.7554/eLife.29236. PMID:28915104 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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