Hexameric molecular motors: P4 packaging ATPase unravels the mechanism.
Cell Mol Life Sci
; 63(10): 1095-105, 2006 May.
Article
en En
| MEDLINE
| ID: mdl-16505972
ABSTRACT
Genome packaging into an empty capsid is an essential step in the assembly of many complex viruses. In double-stranded RNA (dsRNA) bacteriophages of the Cystoviridae family this step is performed by a hexameric helicase P4 which is one of the simplest packaging motors found in nature. Biochemical and structural studies of P4 proteins have led to a surprising finding that these proteins bear mechanistic and structural similarities to a variety of the pervasive RecA/F1-ATPase-like motors that are involved in diverse biological functions. This review describes the role of P4 proteins in assembly, transcription and replication of dsRNA bacteriophages as it has emerged over the past decade while focusing on the most recent structural studies. The P4 mechanism is compared with the models proposed for the related hexameric motors.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Adenosina Trifosfatasas
/
Cystoviridae
/
Ensamble de Virus
/
ARN Helicasas
/
Proteínas Motoras Moleculares
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Cell Mol Life Sci
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2006
Tipo del documento:
Article
País de afiliación:
Finlandia