Structural highlights
Function
MATA_BPMS2 The maturation protein is required for the typical attachment of the phage to the side of the bacterial pili (PubMed:23810697). Binds to sequences located toward each end of the genome, hence circularizing it (PubMed:26608810). The RNA genome-maturation protein A complex is released from the capsid upon host receptor binding (PubMed:23810697). Maturation protein A enters the cell along with the viral RNA (PubMed:4551992).[1] [2] [3]
References
- ↑ Dent KC, Thompson R, Barker AM, Hiscox JA, Barr JN, Stockley PG, Ranson NA. The Asymmetric Structure of an Icosahedral Virus Bound to Its Receptor Suggests a Mechanism for Genome Release. Structure. 2013 Jun 25. pii: S0969-2126(13)00194-9. doi:, 10.1016/j.str.2013.05.012. PMID:23810697 doi:10.1016/j.str.2013.05.012
- ↑ Rolfsson O, Middleton S, Manfield IW, White SJ, Fan B, Vaughan R, Ranson NA, Dykeman E, Twarock R, Ford J, Kao CC, Stockley PG. Direct Evidence for Packaging Signal-Mediated Assembly of Bacteriophage MS2. J Mol Biol. 2016 Jan 29;428(2 Pt B):431-48. doi: 10.1016/j.jmb.2015.11.014. Epub , 2015 Dec 1. PMID:26608810 doi:https://dx.doi.org/10.1016/j.jmb.2015.11.014
- ↑ Krahn PM, O'Callaghan RJ, Paranchych W. Stages in phage R17 infection. VI. Injection of A protein and RNA into the host cell. Virology. 1972 Mar;47(3):628-37. PMID:4551992
