7OZ4
Mature capsid of bacteriophage phiRSA1
Summary for 7OZ4
| Entry DOI | 10.2210/pdb7oz4/pdb |
| EMDB information | 13120 |
| Descriptor | p2 family phage major capsid protein (1 entity in total) |
| Functional Keywords | bacteriophage, capsid, virus |
| Biological source | Ralstonia virus RSA1 |
| Total number of polymer chains | 7 |
| Total formula weight | 264820.72 |
| Authors | Effantin, G.,Fujiwara, A.,Kawsaki, T.,Yamada, T.,Schoehn, G. (deposition date: 2021-06-25, release date: 2021-11-17, Last modification date: 2024-07-17) |
| Primary citation | Effantin, G.,Fujiwara, A.,Kawasaki, T.,Yamada, T.,Schoehn, G. High Resolution Structure of the Mature Capsid of Ralstonia solanacearum Bacteriophage phi RSA1 by Cryo-Electron Microscopy. Int J Mol Sci, 22:-, 2021 Cited by PubMed Abstract: The ϕRSA1 bacteriophage has been isolated from , a gram negative bacteria having a significant economic impact on many important crops. We solved the three-dimensional structure of the ϕRSA1 mature capsid to 3.9 Å resolution by cryo-electron microscopy. The capsid shell, that contains the 39 kbp of dsDNA genome, has an icosahedral symmetry characterized by an unusual triangulation number of T = 7, . The ϕRSA1 capsid is composed solely of the polymerization of the major capsid protein, gp8, which exhibits the typical "Johnson" fold first characterized in bacteriophage HK97. As opposed to the latter, the ϕRSA1 mature capsid is not stabilized by covalent crosslinking between its subunits, nor by the addition of a decoration protein. We further describe the molecular interactions occurring between the subunits of the ϕRSA1 capsid and their relationships with the other known bacteriophages. PubMed: 34681713DOI: 10.3390/ijms222011053 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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