2WBH

Icosahedral particle of covalent coat protein dimer of bacteriophage MS2

Summary for 2WBH

• Entry DOI: 10.2210/pdb2wbh/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 2VTU 5MSF 6MSF 7MSF
• Descriptor: COAT PROTEIN (1 entity in total)
• Functional Keywords: capsid protein, covalent dimer, virion, rna-binding, virus
• Biological source: ENTEROBACTERIA PHAGE MS2
• Total number of polymer chains: 3
• Total formula weight: 82115.63

Authors

Plevka, P.,Tars, K.,Liljas, L. (deposition date: 2009-02-27, release date: 2009-11-24, Last modification date: 2023-12-13)

Primary citation

Plevka, P.,Tars, K.,Liljas, L.
Structure and Stability of Icosahedral Particles of a Covalent Coat Protein Dimer of Bacteriophage MS2.
Protein Sci., 18:1653-, 2009

PubMed Abstract: Particles formed by the bacteriophage MS2 coat protein mutants with insertions in their surface loops induce a strong immune response against the inserted epitopes. The covalent dimers created by fusion of two copies of the coat protein gene are more tolerant to various insertions into the surface loops than the single subunits. We determined a 4.7-A resolution crystal structure of an icosahedral particle assembled from covalent dimers and compared its stability with wild-type virions. The structure resembled the wild-type virion except for the intersubunit linker regions. The covalent dimer orientation was random with respect to both icosahedral twofold and quasi-twofold symmetry axes. A fraction of the particles was unstable in phosphate buffer because of assembly defects. Our results provide a structural background for design of modified covalent coat protein dimer subunits for use in immunization.

PubMed: 19521994
DOI: 10.1002/PRO.184

Experimental method

X-RAY DIFFRACTION (4.7 Å)