Hexameric molecular motors: P4 packaging ATPase unravels the mechanism

Kainov, D E, Tuma, R and Mancini, E J (2006) Hexameric molecular motors: P4 packaging ATPase unravels the mechanism. Cellular and Molecular Life Sciences, 63 (10). pp. 1095-1105. ISSN 1420-682X

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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. © Birkhäuser Verlag, 2006.

Item Type: Article
Schools and Departments: School of Life Sciences > Biochemistry
Subjects: Q Science
Depositing User: Tom Gittoes
Date Deposited: 29 Jan 2015 15:41
Last Modified: 29 Jan 2015 15:41
URI: http://srodev.sussex.ac.uk/id/eprint/52560
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