Liljas L, Fridborg K, Valegård K, Bundule M, Pumpens P
Department of Molecular Biology, Uppsala University, Sweden.
J Mol Biol. 1994 Dec 2;244(3):279-90. doi: 10.1006/jmbi.1994.1729.
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.
细菌病毒fr重组衣壳的结构已通过X射线晶体学在3.5埃分辨率下确定。衣壳是通过在该病毒的天然宿主大肠杆菌中表达fr衣壳蛋白产生的，可能与天然病毒的蛋白外壳基本相同。该结构是使用相关MS2病毒的蛋白外壳通过分子置换确定的，并精修至晶体学R因子为0.228。对这些病毒的蛋白外壳进行比较表明它们非常相似，这表明它们可能对准对称蛋白外壳的组装具有相似的调控机制。
