Structural highlights
Function
[P5_BPPRD] In association with P31 and P2, forms the spike complexes located at the 5-fold vertices of the capsid. Essential for viral infectivity.[1]
Publication Abstract from PubMed
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.
The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture.,Merckel MC, Huiskonen JT, Bamford DH, Goldman A, Tuma R Mol Cell. 2005 Apr 15;18(2):161-70. PMID:15837420[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Caldentey J, Tuma R, Bamford DH. Assembly of bacteriophage PRD1 spike complex: role of the multidomain protein P5. Biochemistry. 2000 Aug 29;39(34):10566-73. PMID:10956048
- ↑ Merckel MC, Huiskonen JT, Bamford DH, Goldman A, Tuma R. The structure of the bacteriophage PRD1 spike sheds light on the evolution of viral capsid architecture. Mol Cell. 2005 Apr 15;18(2):161-70. PMID:15837420 doi:S1097-2765(05)01189-5
