2VTU

crystal structure of bacteriophage MS2 covalent coat protein dimer

Summary for 2VTU

• Entry DOI: 10.2210/pdb2vtu/pdb
• Related: 1AQ3 1AQ4 1BMS 1MSC 1MST 1MVA 1MVB 1U1Y 1ZDH 1ZDI 1ZDJ 1ZDK 1ZSE 2B2D 2B2E 2B2G 2BNY 2BQ5 2BS0 2BS1 2BU1 2C4Q 2C4Y 2C4Z 2C50 2C51 2IZ8 2IZ9 2IZM 2IZN 2MS2 5MSF 6MSF 7MSF
• Descriptor: MS2 COAT PROTEIN (1 entity in total)
• Functional Keywords: ms2, virus, dimer, virion, octahedron, rna-binding, coat protein, capsid protein
• Biological source: ENTEROBACTERIO PHAGE MS2
• Cellular location: Virion (Potential): P03612
• Total number of polymer chains: 2
• Total formula weight: 54743.75

Authors

Plevka, P.,Tars, K.,Liljas, L. (deposition date: 2008-05-15, release date: 2008-08-12, Last modification date: 2023-12-13)

Primary citation

Plevka, P.,Tars, K.,Liljas, L.
Crystal Packing of a Bacteriophage MS2 Coat Protein Mutant Corresponds to Octahedral Particles.
Protein Sci., 17:1731-, 2008

PubMed 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.

PubMed: 18662904
DOI: 10.1110/PS.036905.108

Experimental method

X-RAY DIFFRACTION (3.5 Å)