Terminase: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
The large subunit of Ter is composed of an N-terminal ATPase domain, a linker region and a C-terminal nuclease domain. | The large subunit of Ter is composed of an <scene name='77/775254/Cv/2'>N-terminal ATPase domain, a linker region and a C-terminal nuclease domain</scene>. ATP binds to the protein in a <scene name='77/775254/Cv/4'>groove between the ATPase domain and the linker region</scene><ref>PMID:23630261</ref>. | ||
</StructureSection> | </StructureSection> | ||
== 3D Structures of terminase == | == 3D Structures of terminase == | ||
Revision as of 17:10, 6 December 2017
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. Structural highlightsThe large subunit of Ter is composed of an . ATP binds to the protein in a [2]. |
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3D Structures of terminase3D Structures of terminase
Updated on 06-December-2017
ReferencesReferences
- ↑ Feiss M, Rao VB. The bacteriophage DNA packaging machine. Adv Exp Med Biol. 2012;726:489-509. doi: 10.1007/978-1-4614-0980-9_22. PMID:22297528 doi:http://dx.doi.org/10.1007/978-1-4614-0980-9_22
- ↑ Zhao H, Christensen TE, Kamau YN, Tang L. Structures of the phage Sf6 large terminase provide new insights into DNA translocation and cleavage. Proc Natl Acad Sci U S A. 2013 May 14;110(20):8075-8080. Epub 2013 Apr 29. PMID:23630261 doi:10.1073/pnas.1301133110