1FOQ
PENTAMERIC MODEL OF THE BACTERIOPHAGE PHI29 PROHEAD RNA
Summary for 1FOQ
Entry DOI | 10.2210/pdb1foq/pdb |
Descriptor | BACTERIOPHAGE PHI29 PROHEAD RNA (1 entity in total) |
Functional Keywords | dsrna oligomeric model, prohead rna, bacteriophage phi29, rna |
Biological source | Bacillus phage phi29 |
Total number of polymer chains | 5 |
Total formula weight | 192092.89 |
Authors | Simpson, A.A.,Tao, Y.,Leiman, P.G.,Badasso, M.O.,He, Y.,Jardine, P.J.,Olson, N.H.,Morais, M.C.,Grimes, S.,Anderson, D.L.,Baker, T.S.,Rossmann, M.G. (deposition date: 2000-08-28, release date: 2000-12-22, Last modification date: 2024-02-07) |
Primary citation | Simpson, A.A.,Tao, Y.,Leiman, P.G.,Badasso, M.O.,He, Y.,Jardine, P.J.,Olson, N.H.,Morais, M.C.,Grimes, S.,Anderson, D.L.,Baker, T.S.,Rossmann, M.G. Structure of the bacteriophage phi29 DNA packaging motor. Nature, 408:745-750, 2000 Cited by 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 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. PubMed: 11130079DOI: 10.1038/35047129 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (20 Å) |
Structure validation
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