title: The 2.8 A structure of a T = 4 animal virus and its implications for membrane translocation of RNA.
abstract: Simple RNA animal viruses generally enter cells through receptor-mediated endocytosis followed by acid pH dependent release and translocation of RNA across the endosomal membrane. The T = 3 nodaviruses contain prefabricated pentameric helical bundles that are cleaved from the remainder of the subunits by an assembly-dependent auto-proteolysis and they are positioned for release through 5-fold axes of the particle. We previously proposed that these bundles may serve as conduits for RNA membrane translocation. Additional support for this hypothesis is now provided by the first atomic resolution structure of a T = 4 RNA virus, where we find cleavage sites and helical bundles nearly identical with those observed in T = 3 nodaviruses. The helices are of sufficient length to span a membrane bilayer and the internal diameter of the coiled bundle could accommodate ssRNA. The T = 4 particle has a mean outer diameter of 410 A and is formed by 240 copies of a single subunit type. The subunit is composed of a helical inner domain (where the cleavage occurs) containing residues preceding and following a canonical, viral, eight-stranded beta-sandwich that forms the contiguous shell. Inserted between two strands of the shell domain are 133 residues with an immunoglobulin c-type fold. The initial gene product consists of 644 amino acid residues and is cleaved between residues Asn570 and Phe571 in the mature particle determined in this analysis.
authors: Department of Biological Sciences, Purdue University West Lafayette, Indiana 47907-1392, USA.
authors: S
authors: S
authors: Munshi
authors: L
authors: L
authors: Liljas
authors: J
authors: J
authors: Cavarelli
authors: W
authors: W
authors: Bomu
authors: B
authors: B
authors: McKinney
authors: V
authors: V
authors: Reddy
authors: J E
authors: JE
authors: Johnson
mesh_terms: D001692:Biological Transport; D002213:Capsid / Q000737:chemistry* / Q000378:metabolism; D036022:Capsid Proteins; D002462:Cell Membrane / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D019143:Evolution, Molecular; D005656:Fungal Proteins; D006860:Hydrogen Bonding; D007304:Insect Viruses / Q000737:chemistry* / Q000648:ultrastructure; D008051:Lipid Bilayers; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012328:RNA Viruses / Q000737:chemistry* / Q000648:ultrastructure; D012367:RNA, Viral / Q000378:metabolism
chemical_list: D036022:Capsid Proteins; D005656:Fungal Proteins; D008051:Lipid Bilayers; C094005:NUDC protein, Emericella nidulans; D012367:RNA, Viral; C092202:coat protein, Nudaurelia capensis omega virus