2bpa

Structural highlights

Function

CAPSD_BPPHS Assembles to form an icosahedral capsid with a T=1 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins F (PubMed:11991963, PubMed:1370343, PubMed:8158636). Upon virus binding to host cell, one of the spikes dissociates from the capsid and the virus interacts with LPS through the exposed EF loops on the F proteins (PubMed:29229840). After the genome had been ejected, the channel formed by the F proteins at the unique fivefold axis remains open (PubMed:29229840).^{[1] [2] [3] [4]}

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

1. ↑ Hafenstein S, Fane BA. phi X174 genome-capsid interactions influence the biophysical properties of the virion: evidence for a scaffolding-like function for the genome during the final stages of morphogenesis. J Virol. 2002 Jun;76(11):5350-6. PMID:11991963
2. ↑ McKenna R, Xia D, Willingmann P, Ilag LL, Krishnaswamy S, Rossmann MG, Olson NH, Baker TS, Incardona NL. Atomic structure of single-stranded DNA bacteriophage phi X174 and its functional implications. Nature. 1992 Jan 9;355(6356):137-43. PMID:1370343 doi:http://dx.doi.org/10.1038/355137a0
3. ↑ Sun Y, Roznowski AP, Tokuda JM, Klose T, Mauney A, Pollack L, Fane BA, Rossmann MG. Structural changes of tailless bacteriophage ΦX174 during penetration of bacterial cell walls. Proc Natl Acad Sci U S A. 2017 Dec 26;114(52):13708-13713. PMID:29229840 doi:10.1073/pnas.1716614114
4. ↑ McKenna R, Ilag LL, Rossmann MG. Analysis of the single-stranded DNA bacteriophage phi X174, refined at a resolution of 3.0 A. J Mol Biol. 1994 Apr 15;237(5):517-43. PMID:8158636 doi:10.1006/jmbi.1994.1253