Atomic structure of single-stranded DNA bacteriophage phi X174 and its functional implications. |
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Authors: | 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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Institution: | Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907. |
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Abstract: | 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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