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1FOQ

PENTAMERIC MODEL OF THE BACTERIOPHAGE PHI29 PROHEAD RNA

Summary for 1FOQ
Entry DOI10.2210/pdb1foq/pdb
DescriptorBACTERIOPHAGE PHI29 PROHEAD RNA (1 entity in total)
Functional Keywordsdsrna oligomeric model, prohead rna, bacteriophage phi29, rna
Biological sourceBacillus phage phi29
Total number of polymer chains5
Total formula weight192092.89
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 citationSimpson, 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: 11130079
DOI: 10.1038/35047129
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (20 Å)
Structure validation

226707

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