Summary for 2MS2
| Entry DOI | 10.2210/pdb2ms2/pdb |
| Descriptor | BACTERIOPHAGE MS2 COAT PROTEIN (2 entities in total) |
| Functional Keywords | bacteriophage coat protein, icosahedral virus, virus |
| Biological source | Enterobacterio phage MS2 |
| Cellular location | Virion (Potential): P03612 |
| Total number of polymer chains | 3 |
| Total formula weight | 41215.39 |
| Authors | Valegard, K.,Liljas, L. (deposition date: 1994-08-23, release date: 1995-01-26, Last modification date: 2024-05-22) |
| Primary citation | Golmohammadi, R.,Valegard, K.,Fridborg, K.,Liljas, L. The refined structure of bacteriophage MS2 at 2.8 A resolution. J.Mol.Biol., 234:620-639, 1993 Cited by PubMed Abstract: Bacteriophage MS2 is an icosahedral virus with 180 copies of a coat protein forming a shell around a single-stranded RNA molecule. The coat protein subunits form a lattice with the triangulation number T = 3. The coat protein has a fold which is different from the fold of all other viral coat proteins so far known. It consists of a five-stranded beta sheet facing the inside of the particle, and a hairpin and two helices on the outside. The crystal structure has been refined at 2.8 A resolution. The final R-factor was 0.189 for reflections with F > 2 sigma, and the root-mean-square deviation from idealized bond lengths and bond angles was 0.015 A and 2.9 degrees, respectively. The three chemically identical conformers A, B and C are largely similar. The B conformer has a unique conformation in one loop, which is involved in 5-fold interactions, while the A and C conformers, which are involved in the quasi-6-fold contacts, are similar throughout the structure. One cis-proline has been identified in the B conformer but the corresponding prolines in A and C are of the trans isomer. This residue is conserved within small RNA coliphages and it is proposed that this isomerization enables a less elongated loop (FG) around the 5-fold axis, thus creating a channel. The extensive dimer contact supports the idea of dimers as initial building blocks. An assembly pathway is proposed where five dimers converge into a pentamer and 12 pentamers are linked together with free dimers creating a complete particle. PubMed: 8254664DOI: 10.1006/jmbi.1993.1616 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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