1GW7
QUASI-ATOMIC RESOLUTION MODEL OF BACTERIOPHAGE PRD1 CAPSID, OBTAINED BY COMBINED CRYO-EM AND X-RAY CRYSTALLOGRAPHY.
Summary for 1GW7
| Entry DOI | 10.2210/pdb1gw7/pdb |
| Related | 1CJD 1GW8 1HB5 1HB7 1HQN 1HX6 |
| EMDB information | 1011 |
| Descriptor | MAJOR CAPSID PROTEIN (1 entity in total) |
| Functional Keywords | virus/viral protein, tectiviridae, bacteriophage prd1, cryo- em, image reconstruction, icosahedral virus, virus-viral protein complex |
| Biological source | BACTERIOPHAGE PRD1 |
| Total number of polymer chains | 12 |
| Total formula weight | 520154.63 |
| Authors | San Martin, C.,Huiskonen, J.,Bamford, J.K.H.,Butcher, S.J.,Fuller, S.D.,Bamford, D.H.,Burnett, R.M. (deposition date: 2002-03-08, release date: 2002-03-13, Last modification date: 2024-05-08) |
| Primary citation | San Martin, C.,Huiskonen, J.,Bamford, J.K.H.,Butcher, S.J.,Fuller, S.D.,Bamford, D.H.,Burnett, R.M. Minor Proteins, Mobile Arms, and Membrane-Capsid Interactions in Bacteriophage Prd1 Capsid Assembly Nat.Struct.Biol., 9:756-, 2002 Cited by PubMed Abstract: Bacteriophage PRD1 shares many structural and functional similarities with adenovirus. A major difference is the PRD1 internal membrane, which acts in concert with vertex proteins to translocate the phage genome into the host. Multiresolution models of the PRD1 capsid, together with genetic analyses, provide fine details of the molecular interactions associated with particle stability and membrane dynamics. The N- and C-termini of the major coat protein (P3), which are required for capsid assembly, act as conformational switches bridging capsid to membrane and linking P3 trimers. Electrostatic P3-membrane interactions increase virion stability upon DNA packaging. Newly revealed proteins suggest how the metastable vertex works and how the capsid edges are stabilized. PubMed: 12219080DOI: 10.1038/NSB837 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (13.5 Å) |
Structure validation
Download full validation report
