Structural highlights
Function
BP45_BPMU Component of the baseplate that forms a central needlelike spike used to puncture the host cell membrane for tube insertion during virus entry. Probably involved in baseplate and tail assembly. Serves as the distal plug of tail tube channel and might regulate the process of the phage DNA and protein ejection into the host cell.[1] [2]
References
- ↑ Suzuki H, Yamada S, Toyama Y, Takeda S. The C-terminal domain is sufficient for host-binding activity of the Mu phage tail-spike protein. Biochim Biophys Acta. 2010 Sep;1804(9):1738-42. doi:, 10.1016/j.bbapap.2010.05.003. Epub 2010 May 15. PMID:20478417 doi:http://dx.doi.org/10.1016/j.bbapap.2010.05.003
- ↑ Harada K, Yamashita E, Nakagawa A, Miyafusa T, Tsumoto K, Ueno T, Toyama Y, Takeda S. Crystal structure of the C-terminal domain of Mu phage central spike and functions of bound calcium ion. Biochim Biophys Acta. 2013 Jan;1834(1):284-91. doi: 10.1016/j.bbapap.2012.08.015., Epub 2012 Aug 24. PMID:22922659 doi:http://dx.doi.org/10.1016/j.bbapap.2012.08.015
