Structure of the bacteriophage φ29 DNA packaging motor

Alan A. Simpson, Yizhi Tao, Petr G. Leiman, Mohammed O. Badasso, Yongning He, Paul J. Jardine, Norman H. Olson, Marc C. Morais, Shelley Grimes, Dwight L. Anderson, Timothy S. Baker and Michael G. Rossmann ()
Additional contact information
Alan A. Simpson: Purdue University
Yizhi Tao: Purdue University
Petr G. Leiman: Purdue University
Mohammed O. Badasso: 18-246 Moos Tower, University of Minnesota
Yongning He: Purdue University
Paul J. Jardine: University of New Brunswick
Norman H. Olson: Purdue University
Marc C. Morais: Purdue University
Shelley Grimes: 18-246 Moos Tower, University of Minnesota
Dwight L. Anderson: 18-246 Moos Tower, University of Minnesota
Timothy S. Baker: Purdue University
Michael G. Rossmann: Purdue University

Nature, 2000, vol. 408, issue 6813, 745-750

Abstract: Abstract Motors generating mechanical force, powered by the hydrolysis of ATP, translocate double-stranded DNA into preformed capsids (proheads) of bacterial viruses1,2 and certain animal viruses3. Here we describe the motor that packages the double-stranded DNA of the Bacillus subtilis bacteriophage φ29 into a precursor capsid. We determined the structure of the head–tail connector—the central component of the φ29 DNA packaging motor—to 3.2 Å resolution by means of X-ray crystallography. We then fitted the connector into the electron densities of the prohead and of the partially packaged prohead as determined using cryo-electron microscopy and image reconstruction analysis. Our results suggest that the prohead plus dodecameric connector, prohead RNA, viral ATPase and DNA comprise a rotary motor with the head–prohead RNA–ATPase complex acting as a stator, the DNA acting as a spindle, and the connector as a ball-race. The helical nature of the DNA converts the rotary action of the connector into translation of the DNA.

Date: 2000
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DOI: 10.1038/35047129

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