Tables show that the wheat mosaic virus coat protein has Ca 2+ and Mg 2+ -ATP binding sites. Coat protein stimulates the binding of Mg 2+ -ATP to initiate serine-threonine kinase activity by binding Ca 2+ through an EF-hand. Coating protein with serine kinase activity makes it easier for them to bind chitin, collagen, or fibrillar cellulose. Glycosyl hydrolases and swelling enzymes are activated once the PPM enzyme domain that binds Mg 2+ -ATP is triggered. Since this process involves the hydrolysis of the protein's glycosyl chains, it causes the cell wall to expand. The motor domains of the coat protein then spins and punches holes in the cell wall. In the end, the coat protein creates membrane fusion pores on the cell membrane via phospholipid transporting domains and inserts viral genetic material into plant cells.