Function
Terminase (Ter) is a key component of the DNA packaging machine found in bacteriophages and herpesviruses. The Ter complex is comprised of a small Ter subunit which is a recognition subunit and a large Ter subunit which is an endonuclease/translocase subunit [1]. The nuclease activity of the large Ter subunit is stimulated by ATP. The tripartite terminase complex of herpesvirus which contains 3 subunits (TRM1, TRM2 and TRM3), is found in the cytoplasm of infected cells and uses the cell's import machinery to enter the nucleus[2]. TRM3 has RNase H-like activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genome[3].
Structural highlights
The large subunit of Ter is composed of an . ATP binds to the protein in a [4].
3D Structures of terminase
Terminase 3D Structures
