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This Article ACCEPTED PREPRINT Full Text (PDF) All Versions of this Article: ps.036905.108v1 17/10/1731    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Google Scholar Articles by Plevka, P. Articles by Liljas, L. PubMed PubMed Citation Articles by Plevka, P. Articles by Liljas, L. Social Bookmarking                   What's this?

Crystal packing of a bacteriophage MS2 coat protein mutant corresponds to octahedral particles

¹ Uppsala University;
² Latvian Biomedical Research and Study Centre

(RECEIVED June 9, 2008; ACCEPTED July 22, 2008)

A covalent dimer of the bacteriophage MS2 coat protein was created by 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 artefacts 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 wildtype 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 wildtype 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 four-fold and five-fold symmetry axes where different sets of loops mediate the contacts. The volume of the wildtype virions is 7 times bigger than that of the octahedral particles.

Keywords: Protein Structure/Folding; Virus Proteins; Structure; Viral protein topologies; Crystallography

³ E-mail: pp2cz{at}yahoo.com

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