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Published online before print July 28, 2008, 10.1110/ps.036905.108
Protein Science (2008), 17:1731-1739. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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Crystal packing of a bacteriophage MS2 coat protein mutant corresponds to octahedral particles

Pavel Plevka1, Kaspars Tars2, and Lars Liljas1

1 Department of Cell and Molecular Biology, Uppsala University, SE-751 24 Uppsala, Sweden
2 Latvian Biomedical Research and Study Centre, LV 1067 Riga, Latvia

(RECEIVED June 9, 2008; FINAL REVISION July 21, 2008; ACCEPTED July 22, 2008)

A covalent dimer of the bacteriophage MS2 coat protein was created by performing genetic fusion of two copies of the gene while removing the stop codon of the first gene. The dimer was crystallized in the cubic F432 space group. The organization of the asymmetric unit together with the F432 symmetry results in an arrangement of subunits that corresponds to T = 3 octahedral particles. The octahedral particles are probably artifacts created by the particular crystal packing. When it is not crystallized in the F cubic crystal form, the coat protein dimer appears to assemble into T = 3 icosahedral particles indistinguishable from the wild-type particles. To form an octahedral particle with closed surface, the dimer subunits interact at sharper angles than in the icosahedral arrangement. The fold of the covalent dimer is almost identical to the wild-type dimer with differences located in loops and in the covalent linker region. The main differences in the subunit packing between the octahedral and icosahedral arrangements are located close to the fourfold and fivefold symmetry axes where different sets of loops mediate the contacts. The volume of the wild-type virions is 7 times bigger than that of the octahedral particles.

Keywords: MS2; virus; icosahedron; octahedron; coat protein; dimer


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