Atomic structure of single-stranded DNA bacteriophage ΦX174 and its functional implications
The mechanism of DNA ejection, viral assembly and evolution are related to the structure of bacteriophage ΦX174. The F protein forms a T = 1 capsid whose major folding motif is the eight–stranded antiparallelβ barrel found in many other icosahedral viruses. Groups of 5 G proteins form 12 dominating...
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Veröffentlicht in: | Nature (London) 1992-01, Vol.355 (6356), p.137-143 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The mechanism of DNA ejection, viral assembly and evolution are related to the structure of bacteriophage ΦX174. The F protein forms a
T
= 1 capsid whose major folding motif is the eight–stranded antiparallelβ 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 β 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. |
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ISSN: | 0028-0836 1476-4687 |
DOI: | 10.1038/355137a0 |