Defining Molecular and Domain Boundaries in the Bacteriophage [phi]29 DNA Packaging Motor

Cryo-electron microscopy (cryo-EM) studies of the bacteriophage [phi]29 DNA packaging motor have delineated the relative positions and molecular boundaries of the 12-fold symmetric head-tail connector, the 5-fold symmetric prohead RNA (pRNA), the ATPase that provides the energy for packaging, and th...

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Bibliographic Details
Published in:Structure (London) 2008-08, Vol.16 (8), p.1267-1274
Main Authors: Morais, Marc C, Koti, Jaya S, Bowman, Valorie D, Reyes-Aldrete, Emilio, Anderson, Dwight L, Rossmann, Michael G
Format: Article
Language:English
Subjects:
Bacteria
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Summary:Cryo-electron microscopy (cryo-EM) studies of the bacteriophage [phi]29 DNA packaging motor have delineated the relative positions and molecular boundaries of the 12-fold symmetric head-tail connector, the 5-fold symmetric prohead RNA (pRNA), the ATPase that provides the energy for packaging, and the procapsid. Reconstructions, assuming 5-fold symmetry, were determined for proheads with 174-base, 120-base, and 71-base pRNA; proheads lacking pRNA; proheads with ATPase bound; and proheads in which the packaging motor was missing the connector. These structures are consistent with pRNA and ATPase forming a pentameric motor component around the unique vertex of proheads. They suggest an assembly pathway for the packaging motor and a mechanism for DNA translocation into empty proheads.
ISSN:0969-2126
DOI:10.1016/j.str.2008.05.010