1CJD
THE BACTERIOPHAGE PRD1 COAT PROTEIN, P3, IS STRUCTURALLY SIMILAR TO HUMAN ADENOVIRUS HEXON
Summary for 1CJD
| Entry DOI | 10.2210/pdb1cjd/pdb |
| Descriptor | PROTEIN (MAJOR CAPSID PROTEIN (P3)) (2 entities in total) |
| Functional Keywords | bacteriophage prd1, coat protein, jelly roll, viral protein |
| Biological source | Enterobacteria phage PRD1 |
| Total number of polymer chains | 3 |
| Total formula weight | 130038.66 |
| Authors | Benson, S.D.,Bamford, J.K.H.,Bamford, D.H.,Burnett, R.M. (deposition date: 1999-04-12, release date: 1999-09-20, Last modification date: 2023-12-27) |
| Primary citation | Benson, S.D.,Bamford, J.K.,Bamford, D.H.,Burnett, R.M. Viral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures. Cell(Cambridge,Mass.), 98:825-833, 1999 Cited by PubMed Abstract: The unusual bacteriophage PRD1 features a membrane beneath its icosahedral protein coat. The crystal structure of the major coat protein, P3, at 1.85 A resolution reveals a molecule with three interlocking subunits, each with two eight-stranded viral jelly rolls normal to the viral capsid, and putative membrane-interacting regions. Surprisingly, the P3 molecule closely resembles hexon, the equivalent protein in human adenovirus. Both viruses also have similar overall architecture, with identical capsid lattices and attachment proteins at their vertices. Although these two dsDNA viruses infect hosts from very different kingdoms, their striking similarities, from major coat protein through capsid architecture, strongly suggest their evolutionary relationship. PubMed: 10499799DOI: 10.1016/S0092-8674(00)81516-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
Download full validation report
