Structural highlights
Function
CAPSD_BPFR Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 26 nm in diameter, and consisting of 89 capsid proteins dimers (178 capsid proteins). Involved in viral genome encapsidation through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome. The capsid contains also 1 copy of the A2 maturation protein.[UniProtKB:P03612] Acts as a translational repressor of viral replicase synthesis late in infection. This latter function is the result of capsid protein interaction with an RNA hairpin which contains the replicase ribosome-binding site.[UniProtKB:P03612]
Publication Abstract from PubMed
The structure of recombinant capsids of the bacterial virus fr has been determined by X-ray crystallography at 3.5 A resolution. The capsids were produced by expressing the fr coat protein in Escherichia coli, the natural host of the virus, and are probably essentially identical to the protein shell of the native virus. The structure was determined using molecular replacement with the protein shell of the related MS2 virus, and refined to a crystallographic R-factor of 0.228. A comparison of the protein shells of the viruses shows that they are very similar, and indicates that they may have a similar regulation of the assembly of the quasi-symmetrical protein shell.
Crystal structure of bacteriophage fr capsids at 3.5 A resolution.,Liljas L, Fridborg K, Valegard K, Bundule M, Pumpens P J Mol Biol. 1994 Dec 2;244(3):279-90. PMID:7966339[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liljas L, Fridborg K, Valegard K, Bundule M, Pumpens P. Crystal structure of bacteriophage fr capsids at 3.5 A resolution. J Mol Biol. 1994 Dec 2;244(3):279-90. PMID:7966339 doi:http://dx.doi.org/S0022-2836(84)71729-3
