1YQ5

PRD1 vertex protein P5

Summary for 1YQ5

• Entry DOI: 10.2210/pdb1yq5/pdb
• Related: 1YQ6 1YQ8
• Descriptor: Minor capsid protein (2 entities in total)
• Functional Keywords: beta-spiral, beta-jelly-roll, viral protein
• Biological source: Enterobacteria phage PRD1
• Cellular location: Virion: P22536
• Total number of polymer chains: 2
• Total formula weight: 29188.59

Authors

Merckel, M.C.,Huiskonen, J.T.,Goldman, A.,Bamford, D.H.,Tuma, R. (deposition date: 2005-02-01, release date: 2005-04-26, Last modification date: 2011-07-13)

Primary citation

Merckel, M.C.,Huiskonen, J.T.,Bamford, D.H.,Goldman, A.,Tuma, R.
The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture.
Mol.Cell, 18:161-170, 2005

PubMed Abstract: Comparisons of bacteriophage PRD1 and adenovirus protein structures and virion architectures have been instrumental in unraveling an evolutionary relationship and have led to a proposal of a phylogeny-based virus classification. The structure of the PRD1 spike protein P5 provides further insight into the evolution of viral proteins. The crystallized P5 fragment comprises two structural domains: a globular knob and a fibrous shaft. The head folds into a ten-stranded jelly roll beta barrel, which is structurally related to the tumor necrosis factor (TNF) and the PRD1 coat protein domains. The shaft domain is a structural counterpart to the adenovirus spike shaft. The structural relationships between PRD1, TNF, and adenovirus proteins suggest that the vertex proteins may have originated from an ancestral TNF-like jelly roll coat protein via a combination of gene duplication and deletion.

PubMed: 15837420
DOI: 10.1016/j.molcel.2005.03.019

Experimental method

X-RAY DIFFRACTION (2 Å)