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TitleViral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures.
Journal, issue, pagesCell, Vol. 98, Issue 6, Page 825-833, Year 1999
Publish dateSep 17, 1999
AuthorsS D Benson / J K Bamford / D H Bamford / R M Burnett /
PubMed AbstractThe 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 ...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.
External linksCell / PubMed:10499799
MethodsX-ray diffraction
Resolution1.85 Å
Structure data

PDB-1cjd:
THE BACTERIOPHAGE PRD1 COAT PROTEIN, P3, IS STRUCTURALLY SIMILAR TO HUMAN ADENOVIRUS HEXON
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • enterobacteria phage prd1 (virus)
KeywordsVIRAL PROTEIN / BACTERIOPHAGE PRD1 / COAT PROTEIN / JELLY ROLL

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