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-Structure paper
| Title | Structure of the bacteriophage phi29 DNA packaging motor. |
|---|---|
| Journal, issue, pages | Nature, Vol. 408, Issue 6813, Page 745-750, Year 2000 |
| Publish date | Dec 7, 2000 |
 Authors | A A Simpson / Y Tao / P G Leiman / M O Badasso / Y He / P J Jardine / N H Olson / M C Morais / S Grimes / D L Anderson / T S Baker / M G Rossmann /  |
| PubMed Abstract | Motors generating mechanical force, powered by the hydrolysis of ATP, translocate double-stranded DNA into preformed capsids (proheads) of bacterial viruses and certain animal viruses. Here we ...Motors generating mechanical force, powered by the hydrolysis of ATP, translocate double-stranded DNA into preformed capsids (proheads) of bacterial viruses and certain animal viruses. Here we describe the motor that packages the double-stranded DNA of the Bacillus subtilis bacteriophage phi29 into a precursor capsid. We determined the structure of the head-tail connector--the central component of the phi29 DNA packaging motor--to 3.2 A 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. |
 External links | Nature / PubMed:11130079 / PubMed Central |
| Methods | EM (single particle) / X-ray diffraction |
| Resolution | 3.2 - 20 Å |
| Structure data |  PDB-1foq:  PDB-1fou: |
| Source |
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 Keywords |  RNA / dsRNA oligomeric model / Prohead RNA / Bacteriophage phi29 / VIRAL PROTEIN / alpha-helical barrel |
