Structural highlights
Function
PKG16_BPPH2 ATPase required for the genome encapsidation reaction. Part of the active packaging motor via the binding to the packaging RNA (pRNA), itself fixed to the head-tail connector at the unique portal vertex of the prohead. Binds and supercoils the DNA-gp3 to produce an initiation complex for DNA packaging. Provides the energy to actively pump the viral DNA into the prohead. Approximately one molecule of ATP is used in the packaging of 2 bp of viral DNA. After packaging, the ATPase and the pRNA are released from the prohead.[1] [2] [3] [4]
References
- ↑ Simpson AA, Tao Y, Leiman PG, Badasso MO, He Y, Jardine PJ, Olson NH, Morais MC, Grimes S, Anderson DL, Baker TS, Rossmann MG. Structure of the bacteriophage phi29 DNA packaging motor. Nature. 2000 Dec 7;408(6813):745-50. PMID:11130079 doi:10.1038/35047129
- ↑ Koti JS, Morais MC, Rajagopal R, Owen BA, McMurray CT, Anderson DL. DNA packaging motor assembly intermediate of bacteriophage phi29. J Mol Biol. 2008 Sep 19;381(5):1114-32. doi: 10.1016/j.jmb.2008.04.034. Epub 2008, Apr 20. PMID:18674782 doi:https://dx.doi.org/10.1016/j.jmb.2008.04.034
- ↑ Guo P, Peterson C, Anderson D. Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage phi 29. J Mol Biol. 1987 Sep 20;197(2):229-36. doi: 10.1016/0022-2836(87)90121-5. PMID:2960820 doi:https://dx.doi.org/10.1016/0022-2836(87)90121-5
- ↑ Garvey KJ, Saedi MS, Ito J. The complete sequence of Bacillus phage phi 29 gene 16: a protein required for the genome encapsidation reaction. Gene. 1985;40(2-3):311-6. PMID:3879485
