Structural highlights
Function[VG08_BPP22] Required for successful condensation of DNA within the capsid. The interior of the prohead is filled with the gp8 protein. The scaffolding protein is lost from the structure during packaging. Publication Abstract from PubMedScaffolding proteins are required for high fidelity assembly of most high T number dsDNA viruses such as the large bacteriophages, and the herpesvirus family. They function by transiently binding and positioning the coat protein subunits during capsid assembly. In both bacteriophage P22 and the herpesviruses the extreme scaffold C terminus is highly charged, is predicted to be an amphipathic alpha-helix, and is sufficient to bind the coat protein, suggesting a common mode of action. NMR studies show that the coat protein-binding domain of P22 scaffolding protein exhibits a helix-loop-helix motif stabilized by a hydrophobic core. One face of the motif is characterized by a high density of positive charges that could interact with the coat protein through electrostatic interactions. Results from previous studies with a truncation fragment and the observed salt sensitivity of the assembly process are explained by the NMR structure. Structure of the coat protein-binding domain of the scaffolding protein from a double-stranded DNA virus.,Sun Y, Parker MH, Weigele P, Casjens S, Prevelige PE Jr, Krishna NR J Mol Biol. 2000 Apr 14;297(5):1195-202. PMID:10764583[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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