Each row contains the following information: The graphic that is shown by default represents the longest sequence Internal database links Similarity to PfamA using HHSearch: 2007 26:1984-1994.: Structural framework for DNA translocation via the viral portal protein. Lebedev AA, Krause MH, Isidro AL, Vagin AA, Orlova EV, Turner J, Dodson EJ, Tavares P, Antson AA, EMBO J. 2015 112:7009-7014.: Structural rearrangements in the phage head-to-tail interface during assembly and infection. Lurz R, Orlova EV, Gunther D, Dube P, Droge A, Weise F, van Heel M, Tavares P, J Mol Biol 2001 310:1027-1037.: Structural organisation of the head-to-tail interface of a bacterial virus.Ĭhaban Y, Lurz R, Brasiles S, Cornilleau C, Karreman M, Zinn-Justin S, Tavares P, Orlova EV, Proc Natl Acad Sci U S A. RC Paper describing PDB structure 2jes Literature references This family also includes the old Pfam family Phage_min_cap ( PF:PF05126). It is also found in a number of bacterial species. This protein is common to Siphoviridae (phages with long non-contractile tails) and Myoviridae (phages with contractile tails). In the mature SPP1 virion, Gp6 exists as a dodecamer, while recombinant SPP1 Gp6 has been shown to form 13-subunit assemblies. During SPP1 morphogenesis, the portal protein, Gp6, participates in the procapsid assembly reaction. It also forms the junction between the phage head (capsid) and the tail proteins.
This bacteriophage protein forms a gateway that enables DNA passage during packaging and ejection of the phage genome.
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