Structure，Vol 16, 1267-1274, 06 August 2008，Marc C. Morais, Michael G. Rossmann
Defining Molecular and Domain Boundaries in the Bacteriophage 29 DNA Packaging Motor
Marc C. Morais, Jaya S. Koti,Valorie D. Bowman,Emilio Reyes-Aldrete,Dwight L. Anderson,and Michael G. Rossmann
Cryo-electron microscopy (cryo-EM) studies of the bacteriophage 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.