2wbh

Icosahedral particle of covalent coat protein dimer of bacteriophage MS2

spinqualitylabelsall models 2wbh, resolution 4.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2wbh is a 3 chain structure with sequence from Bpms2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2b2e, 6msf, 2bs0, 2iz9, 7msf, 2b2g, 2c4q, 2c4y, 1zdj, 2c4z, 2c51, 2bny, 1u1y, 2vtu, 2bs1, 1msc, 1mvb, 2izn, 1mst, 1aq4, 2ms2, 2c50, 1zdi, 1zdk, 1aq3, 1mva, 5msf, 2b2d, 1bms, 1zdh, 1zse, 2bq5, 2iz8, 2izm, 2bu1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [COAT_BPMS2] Forms the phage shell; binds to the phage RNA. Publication Abstract from PubMed 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. Structure and stability of icosahedral particles of a covalent coat protein dimer of bacteriophage MS2.,Plevka P, Tars K, Liljas L Protein Sci. 2009 Aug;18(8):1653-61. PMID:19521994 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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