Defining Molecular and Domain Boundaries in the Bacteriophage ϕ29 DNA Packaging Motor

Marc C. Morais, Jaya S. Koti, Valorie D. Bowman, Emilio Reyes-Aldrete, Dwight L. Anderson, Michael G. Rossmann

Research output: Contribution to journalArticlepeer-review

80 Scopus citations


Cryo-electron microscopy (cryo-EM) studies of the bacteriophage φ{symbol}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.

Original languageEnglish (US)
Pages (from-to)1267-1274
Number of pages8
Issue number8
StatePublished - Aug 6 2008



ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


Dive into the research topics of 'Defining Molecular and Domain Boundaries in the Bacteriophage ϕ29 DNA Packaging Motor'. Together they form a unique fingerprint.

Cite this