Viral Evolution Revealed by Bacteriophage PRD1 and Human Adenovirus Coat Protein Structures

The unusual bacteriophage PRD1 features a membrane beneath its icosahedral protein coat. The crystal structure of the major coat protein, P3, at 1.85 Å resolution reveals a molecule with three interlocking subunits, each with two eight-stranded viral jelly rolls normal to the viral capsid, and putat...

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Bibliographic Details
Published inCell Vol. 98; no. 6; pp. 825 - 833
Main Authors Benson, Stacy D, Bamford, Jaana K.H, Bamford, Dennis H, Burnett, Roger M
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 17.09.1999
Subjects
Adenoviruses, Human - chemistry
Amino Acid Sequence
Capsid - chemistry
Capsid Proteins
Crystallization
Crystallography, X-Ray
Evolution, Molecular
Human adenovirus
Models, Molecular
Molecular Sequence Data
Phage PRD1
Protein Conformation
Space life sciences
Synchrotrons
Tectiviridae - chemistry
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Summary:The unusual bacteriophage PRD1 features a membrane beneath its icosahedral protein coat. The crystal structure of the major coat protein, P3, at 1.85 Å 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.
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ISSN:0092-8674
1097-4172
DOI:10.1016/S0092-8674(00)81516-0