Summary for 4BP7
| Entry DOI | 10.2210/pdb4bp7/pdb |
| EMDB information | 2365 |
| Descriptor | COAT PROTEIN (1 entity in total) |
| Functional Keywords | virus, bacteriophage |
| Biological source | ENTEROBACTERIA PHAGE MS2 |
| Cellular location | Virion : P03612 |
| Total number of polymer chains | 180 |
| Total formula weight | 2472923.52 |
| Authors | Dent, K.C.,Thompson, R.,Barker, A.M.,Barr, J.N.,Hiscox, J.A.,Stockley, P.G.,Ranson, N.A. (deposition date: 2013-05-23, release date: 2013-07-17, Last modification date: 2024-05-08) |
| Primary citation | Dent, K.C.,Thompson, R.,Barker, A.M.,Hiscox, J.A.,Barr, J.N.,Stockley, P.G.,Ranson, N.A. The Asymmetric Structure of an Icosahedral Virus Bound its Receptor Suggests a Mechanism for Genome Release. Structure, 21:1225-1234, 2013 Cited by PubMed Abstract: Simple, spherical RNA viruses have well-understood, symmetric protein capsids, but little structural information is available for their asymmetric components, such as minor proteins and their genomes, which are vital for infection. Here, we report an asymmetric structure of bacteriophage MS2, attached to its receptor, the F-pilus. Cryo-electron tomography and subtomographic averaging of such complexes result in a structure containing clear density for the packaged genome, implying that the conformation of the genome is the same in each virus particle. The data also suggest that the single-copy viral maturation protein breaks the symmetry of the capsid, occupying a position that would be filled by a coat protein dimer in an icosahedral shell. This capsomere can thus fulfill its known biological roles in receptor and genome binding and suggests an exit route for the genome during infection. PubMed: 23810697DOI: 10.1016/J.STR.2013.05.012 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (39 Å) |
Structure validation
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