Structural highlights
Function
GP13_BPPH2 May serve as a plug to restrain the highly pressurized packaged genome and thus would be the first virion protein to contact the host cell wall, degrading the peptidoglycan layer and thereby facilitating viral genome entry into the host bacteria. Acts probably as a multifunctional enzyme that degrades N-acetylglucosamine polymers (in vitro) and cleaves the peptide cross-links of the host cell wall. Essential for the tail assembly.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Cohen DN, Erickson SE, Xiang Y, Rossmann MG, Anderson DL. Multifunctional roles of a bacteriophage phi 29 morphogenetic factor in assembly and infection. J Mol Biol. 2008 May 9;378(4):804-17. doi: 10.1016/j.jmb.2008.02.068. Epub 2008, Mar 7. PMID:18394643 doi:http://dx.doi.org/10.1016/j.jmb.2008.02.068
- ↑ Xiang Y, Morais MC, Cohen DN, Bowman VD, Anderson DL, Rossmann MG. Crystal and cryoEM structural studies of a cell wall degrading enzyme in the bacteriophage phi29 tail. Proc Natl Acad Sci U S A. 2008 Jul 15;105(28):9552-7. Epub 2008 Jul 7. PMID:18606992
