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J. Biol. Chem., Vol. 276, Issue 49, 46187-46195, December 7, 2001

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Solution Structure of Bacteriophage PRD1 Vertex Complex^*

Anna Sokolova^§, Marc Malfois^§¶, Javier Caldentey^**, Dmitri I. Svergun^§, Michel H. J. Koch^§, Dennis H. Bamford, and Roman Tuma

From the  Institute of Crystallography, Russian Academy of Sciences, Moscow 117333, Russia, ^§ European Molecular Biology Laboratory, Hamburg Outstation, EMBL c/o DESY, Hamburg D-22603, Germany,  Institute of Biotechnology and Department of Biosciences, Viikki Biocenter, P. O. Box 56 (Viikinkaari 5), University of Helsinki, Helsinki 00014, Finland

Bacteriophage PRD1 is a prototype of viruses with an internal membrane. The icosahedral capsid and major coat protein share structural similarity with the corresponding structures of adenovirus. The present study further explores similarities between these viruses, considering the 5-fold vertex assemblies. The vertex structure of bacteriophage PRD1 consists of proteins P2, P5, and P31. The vertex complex mediates host cell binding and controls double-stranded DNA delivery. Quaternary structures and interactions of purified spike proteins were studied by synchrotron radiation x-ray solution scattering. Low resolution models of the vertex proteins P5, P2, and P31 were reconstructed ab initio from the scattering data. Protein P5 is a long trimer that resembles the adenovirus spike protein pIV. The receptor-binding protein P2 is a 15.5-nm long, thin monomer and does not have an adenovirus counterpart. P31 forms a pentameric base with a maximum diameter of 8.5 nm, which is thinner than the adenovirus penton pIII. P5 further polymerize into a nonameric form ((P5₃)₃). In the presence of P31, P5 associates into a P5₆:P31 complex. The constructed models of these assemblies provided support for a model of vertex assembly onto the virion. Although similar in overall architecture, clear differences between PRD1 and adenovirus spike assemblies have been revealed.

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