4v9e

Crystal Structure of Rift Valley Fever Virus Nucleocapsid Protein Hexamer Bound to Single-stranded RNA.

spinqualitylabelsall models 4v9e, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4v9e is a 42 chain structure. This structure supersedes and combines the now removed PDB entries 4h6f and 4h6g. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4h6f, 4h6g, 4h5l, 4h5m, 4h5o, 4h5p, 4h5q Resources: FirstGlance, OCA, RCSB, PDBsum Warning: this is a large structure, and loading might take a long time or not happen at all. Publication Abstract from PubMed Rift Valley fever and Toscana viruses are human pathogens for which no effective therapeutics exist. These and other phleboviruses have segmented negative-sense RNA genomes that are sequestered by a nucleocapsid protein (N) to form ribonucleoprotein (RNP) complexes of irregular, asymmetric structure, previously uncharacterized at high resolution. N binds nonspecifically to single-stranded RNA with nanomolar affinity. Crystal structures of Rift Valley fever virus N-RNA complexes reconstituted with defined RNAs of different length capture tetrameric, pentameric and hexameric N-RNA multimers. All N-N subunit contacts are mediated by a highly flexible alpha-helical arm. Arm movement gives rise to the three multimers in the crystal structures and also explains the asymmetric architecture of the RNP. Despite the flexible association of subunits, the crystal structures reveal an invariant, monomeric RNP building block, consisting of the core of one N subunit, the arm of a neighboring N, and four RNA nucleotides with the flanking phosphates. Up to three additional RNA nucleotides bind between subunits. The monomeric building block is matched in size to the repeating unit in viral RNP, as visualized by electron microscopy. N sequesters four RNA bases in a narrow hydrophobic binding slot and has polar contacts only with the sugar-phosphate backbone, which faces the solvent. All RNA bases, whether in the binding slot or in the subunit interface, face the protein in a manner that is incompatible with base pairing or with "reading" by the viral polymerase. Phleboviruses encapsidate their genomes by sequestering RNA bases.,Raymond DD, Piper ME, Gerrard SR, Skiniotis G, Smith JL Proc Natl Acad Sci U S A. 2012 Nov 5. PMID:23129612 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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