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

PLEVKA, Pavel, Kaspars TARS and Lars LILJAS. Crystal packing of a bacteriophage MS2 coat protein mutant corresponds to octahedral particles. Protein Science. MALDEN: WILEY-BLACKWELL, 2008, vol. 17, No 10, p. 1731-1739. ISSN 0961-8368. Available from: https://dx.doi.org/10.1110/ps.036905.108.

Basic information

• Original name: Crystal packing of a bacteriophage MS2 coat protein mutant corresponds to octahedral particles
• Authors: PLEVKA, Pavel, Kaspars TARS and Lars LILJAS.
• Edition: Protein Science, MALDEN, WILEY-BLACKWELL, 2008, 0961-8368.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10600 1.6 Biological sciences
• Country of publisher: United States of America
• Confidentiality degree: is not subject to a state or trade secret
• Impact factor: Impact factor: 3.115
• Organization unit: Central European Institute of Technology
• Doi: http://dx.doi.org/10.1110/ps.036905.108
• UT WoS: 000259401900010
• Keywords in English: MS2; virus; icosahedron; octahedron; coat protein; dimer
• Tags: neMU

Abstract

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.