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
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- Small terminase
- 3n4p, 3n4q – Ter nuclease domain – Herpesvirus
- 3hef – Ter – Bacteriophage T7
- 4zc3, 2cmp – Sf6Ter nuclease domain – Bacteriophage Sf6
- 4dyc, 4dzj, 4dzp – Sf6Ter nuclease domain (mutant)
- 3zqp, 3zqm, 3zqn, 3zqo – Sf6Ter oligomerization domain
- 3zqq, 4dyq, 4dyr – Sf6Ter
- 1j9i – Ter nuclease domain – Bacteriophage λ - NMR
- 4xvn – G20cTer nuclease domain – Bacteriophage G20c
- 3p9a – Ter – Bacteriophage P22
- Large terminase
- 4dkw – Ter nuclease domain – Bacteriophage P22
- 4bij, 4bil – T7Ter – Bacteriophage T7 – Cryo EM
- 4idh – T7Ter
- 2wbn, 2wc9 – Ter nuclease domain – Bacteriophage Spp1
- 3c6a, 3c6h – Ter nuclease domain – Bacteriophage Rb49
- 5c10, 5c12 – Sf6Ter nuclease domain
- 5c2d, 5c15 – Sf6Ter nuclease domain (mutant)
- 5m1f, 5m1k, 5m1n, 5m1o, 5m1p, 5m1q – G20cTer
- 5oe8, 5oee, 5oe9 – D6eTer – Bacteriophage D6e
- 5tge – P74Ter nuclease domain – Thermus phage P74
- 4zni, 4znk – P74Ter ATPase domain
- 4znj – P74Ter ATPase domain (mutant)
- 4znl – P74Ter ATPase domain + ADP
- Large terminase complex
- 4iee, 4ife – Sf6Ter + ATP
- 4iei – Sf6Ter + ADP
- 5c2f – Sf6Ter nuclease domain (mutant) + antifungal drug
- 5oea – D6eTer + ATP
- 5oeb – D6eTer + ADP
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
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