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 journalArticle

Abstract

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
JournalStructure
Volume16
Issue number8
DOIs
StatePublished - Aug 6 2008

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Keywords

  • MICROBIO
  • PROTEIN

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Morais, M. C., Koti, J. S., Bowman, V. D., Reyes-Aldrete, E., Anderson, D. L., & Rossmann, M. G. (2008). Defining Molecular and Domain Boundaries in the Bacteriophage ϕ29 DNA Packaging Motor. Structure, 16(8), 1267-1274. https://doi.org/10.1016/j.str.2008.05.010