Crystallization and preliminary X-ray analysis of receptor-binding protein P2 of bacteriophage PRD1.
Bacteriophage PRD1 has remarkable structural similarities to adenovirus, but is unusual in containing a membrane beneath its icosahedral capsid. Its monomeric receptor-binding protein, P2, is part of a complex at each capsid vertex and so is the functional equivalent of adenovirus fiber. P2 has been crystallized by the "hanging-drop" method of vapor diffusion and two different crystal forms were obtained. Macroseeding, used to increase the size of the initial small needles, gave rod-shaped crystals. These grew to a size of 0.08 x 0.08 x 0.50 mm(3) and diffracted to 2.6 A resolution. They have the orthorhombic space group P222(1), with unit cell dimensions a = 137.8 A, b = 46.5 A, c = 136.4 A. A few single crystals of a second form were grown without seeding under slightly different conditions. A parallelepiped crystal (0.10 x 0.10 x 0.35 mm(3)), with space group C222(1) and unit cell dimensions a = 182.3 A, b = 204.8 A, c = 133.3 A, diffracted to 3.5 A resolution. A rotation function for the second form revealed that four monomers of P2 are related by a noncrystallographic twofold axis. The structure of P2 will reveal how this arrangement relates to the trimeric adenovirus fiber.
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The Wistar Institute, 3601 Spruce Street, Philadelphia, Pennsylvania, 19104, USA.
Butcher
S J
SJ
Benson
S D
SD
Bamford
D H
DH
Burnett
R M
RM
D002213:Capsid / Q000737:chemistry*; D036022:Capsid Proteins; D003460:Crystallization; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017916:Tectiviridae / Q000737:chemistry*; D014961:X-Ray Diffraction
D036022:Capsid Proteins; C018315:hexon capsid protein, Adenovirus