Crystallization of the avian reovirus double-stranded RNA-binding and core protein sigmaA.
The avian reovirus protein sigmaA plays a dual role: it is a structural protein forming part of the transcriptionally active core, but it has also been implicated in the resistance of the virus to interferon by strongly binding double-stranded RNA and thus inhibiting the double-stranded RNA-dependent protein kinase. The sigmaA protein has been crystallized from solutions containing ammonium sulfate at pH values around 6. Crystals belonging to space group P1, with unit-cell parameters a = 103.2, b = 129.9, c = 144.0 A, alpha = 93.8, beta = 105.1, gamma = 98.2 degrees were grown and a complete data set has been collected to 2.3 A resolution. The self-rotation function suggests that sigmaA may form symmetric arrangements in the crystals.
Hermo-Parrado
X Lois
XL
Departamento de Bioquímica y Biología Molecular, Facultad de Farmacia, Universidad de Santiago de Compostela, Campus Sur, E-15782 Santiago de Compostela, Spain.
Guardado-Calvo
Pablo
P
Llamas-Saiz
Antonio L
AL
Fox
Gavin C
GC
Vazquez-Iglesias
Lorena
L
Martínez-Costas
José
J
Benavente
Javier
J
van Raaij
Mark J
MJ
D003460:Crystallization; D018360:Crystallography, X-Ray; D030101:Orthoreovirus, Avian / Q000737:chemistry*; D011487:Protein Conformation; D016601:RNA-Binding Proteins / Q000737:chemistry*; D014758:Viral Core Proteins / Q000737:chemistry*
D016601:RNA-Binding Proteins; D014758:Viral Core Proteins; C403292:sigmaA protein, avian reovirus