The 2.8 angstrom structure of a T=4 animal virus and its implications for membrane translocation of RNA

被引:86
作者
Munshi, S [1 ]
Liljas, L [1 ]
Cavarelli, J [1 ]
Bomu, W [1 ]
McKinney, B [1 ]
Reddy, V [1 ]
Johnson, JE [1 ]
机构
[1] PURDUE UNIV, DEPT BIOL SCI, W LAFAYETTE, IN 47907 USA
关键词
viruses; jelly-roll; tetraviruses; Ig-fold; quasi-equivalence; membrane translocation;
D O I
10.1006/jmbi.1996.0437
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom 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. (C) 1996 Academic Press Limited.
引用
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页码:1 / 10
页数:10
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