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

PLEVKA, Pavel, Kaspars TARS a Lars LILJAS. Crystal packing of a bacteriophage MS2 coat protein mutant corresponds to octahedral particles. Protein Science. MALDEN: WILEY-BLACKWELL, 2008, roč. 17, č. 10, s. 1731-1739. ISSN 0961-8368. Dostupné z: https://dx.doi.org/10.1110/ps.036905.108.

Základní údaje

Originální název

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

Autoři

PLEVKA, Pavel, Kaspars TARS a Lars LILJAS

Vydání

Protein Science, MALDEN, WILEY-BLACKWELL, 2008, 0961-8368

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Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 3.115

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1110/ps.036905.108

UT WoS

000259401900010

Klíčová slova anglicky

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

Štítky

neMU

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Anotace

V originále

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.