Terminase
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FunctionTerminase (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 highlightsThe large subunit of Ter is composed of an N-terminal ATPase domain, a linker region and a C-terminal nuclease domain. ATP binds to the protein in a groove between the ATPase domain and the linker region[4]. 3D Structures of terminase
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This page was last modified 07:52, 18 August 2024.