12-Fold symmetry of the putative portal protein from the Thermus thermophilus bacteriophage G20C determined by X-ray analysis.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 69(Pt 11): 1239-41, 2013 Nov.
Article
en En
| MEDLINE
| ID: mdl-24192358
ABSTRACT
In tailed bacteriophages and several animal viruses, the portal protein forms the gateway through which viral DNA is translocated into the head structure during viral particle assembly. In the mature virion the portal protein exists as a dodecamer, while recombinant portal proteins from several phages, including SPP1 and CNPH82, have been shown to form 13-subunit assemblies. A putative portal protein from the thermostable bacteriophage G20C has been cloned, overexpressed and purified. Crystals of the protein diffracted to 2.1â
Å resolution and belonged to space group P42(1)2, with unit-cell parameters a = b = 155.3, c = 115.4â
Å. The unit-cell content and self-rotation function calculations indicate that the protein forms a circular 12-subunit assembly.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Bacteriófagos
/
Thermus thermophilus
/
Proteínas de la Cápside
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Año:
2013
Tipo del documento:
Article
País de afiliación:
Reino Unido