HK96 virus Escher schwan fold

La cápside del virus bacteriofago HK97 esta compuesto por 420 proteínas iguales ensambladas como 60 hexámeros (Naranja-blanco) y 12 pentámeros (Rojos). Este tipo de plegamiento o estructura lo comparten las cápsides de muchos otros virus bacteriofagos- T, fagos lamda e incluso las cápsides de virus eucarióticos como los herpesvirus. La estructura se puede representar artísticamente como un icosaedro compuesto por 420 proteínas en forma de unos cisnes muy peculiares, la naturaleza guarda muchas sorpresas.

The HK97 capsid is formed by the arrangement of 420 protein chains into 60 hexamers (Orange-white) and 12 pentamers (Red). The HK97 fold is present not only in a large number of dsDNA bacteriophage capsids, including the T-phages, lambdoid phages, etc, but also in the major capsid protein of eukaryotic herpesviruses. it seems like an escher icosahedron.

The HK97 capsid is formed by the arrangement of 420 protein chains into 60 hexamers (Orange-white) and 12 pentamers (Red). The HK97 fold is present not only in a large number of dsDNA bacteriophage capsids, including the T-phages, lambdoid phages, etc, but also in the major capsid protein of eukaryotic herpesviruses. it seems like an escher icosahedron.

The HK97 capsid is formed by the arrangement of 420 protein chains into 60 hexamers (Orange-white) and 12 pentamers (Red). The HK97 fold is present not only in a large number of dsDNA bacteriophage capsids, including the T-phages, lambdoid phages, etc, but also in the major capsid protein of eukaryotic herpesviruses. It seems like an escher icosahedron.

REFERENCES

A new topology of the HK97-like fold revealed in Bordetella bacteriophage by cryoEM at 3.5 Å resolution. Xing Zhang, Huatao Guo, Lei Jin, Elizabeth Czornyj, Asher Hodes, Wong H Hui, Angela W Nieh, Jeff F Miller, Z Hong Zhou. University of California, Los Angeles, United States. eLife 2013;2:e01299

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