The characterization and crystallization of a virally encoded Ustilago maydis KP4 toxin.
KP4 is a virally encoded and highly specific toxin that kills fungi closely related to the fungus Ustilago maydis. The toxin was purified and crystals were formed using ammonium sulfate as precipitant. The crystals belong to the space group P6(1)(5)22 and diffracted to approximately 2.2 A resolution. Circular dicroism spectroscopy suggests that the protein is predominantly comprised of beta-strands.
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Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.
Sullivan
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Che
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Ganesa
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Flurkey
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Bozarth
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Smith
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D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000737:chemistry* / Q000302:isolation & purification; D008970:Molecular Weight; D009183:Mycotoxins / Q000737:chemistry* / Q000302:isolation & purification; D017433:Protein Structure, Secondary; D014588:Ustilago / Q000378:metabolism*; D014764:Viral Proteins
D005656:Fungal Proteins; D009183:Mycotoxins; D014764:Viral Proteins; C086592:Ustilago maydis viral toxin KP4