ATOMIC-STRUCTURE OF SINGLE-STRANDED-DNA BACTERIOPHAGE-PHI-X174 AND ITS FUNCTIONAL IMPLICATIONS

Article

关键词: CELL-WALL LIPOPOLYSACCHARIDE;    TOBACCO MOSAIC-VIRUS;    BUSHY STUNT VIRUS;    NUCLEOTIDE-SEQUENCE;    CRYSTAL-STRUCTURE;    2.8-A RESOLUTION;    ANTIVIRAL AGENTS;    PROTEIN;    PHI-X174;    ECLIPSE;   

DOI  :  10.1038/355137a0

来源: SCIE

【 摘 要 】

The mechanism of DNA ejection, viral assembly and evolution are related to the structure of bacteriophage PHI-X174. The F protein forms a T = 1 capsid whose major folding motif is the eight-stranded antiparallel-beta-barrel found in many other icosahedral viruses. Groups of 5 G proteins form 12 dominating spikes that enclose a hydrophilic channel containing some diffuse electron density. Each G protein is a tight-beta-barrel with its strands running radially outwards and with a topology similar to that of the F protein. The 12 'pilot' H proteins per virion may be partially located in the putative ion channel. The small, basic J protein is associated with the DNA and is situated in an interior cleft of the F protein. Tentatively, there are three regions of partially ordered DNA structure, accounting for about 12% of the total genome.

【 授权许可】

Free