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Title
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Atomic structure of single-stranded DNA bacteriophage phi X174 and its functional implications.
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Authors
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R.McKenna,
D.Xia,
P.Willingmann,
L.L.Ilag,
S.Krishnaswamy,
M.G.Rossmann,
N.H.Olson,
T.S.Baker,
N.L.Incardona.
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Ref.
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Nature, 1992,
355,
137-143.
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PubMed id
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Abstract
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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,
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