1FOU

CONNECTOR PROTEIN FROM BACTERIOPHAGE PHI29

Summary for 1FOU

• Entry DOI: 10.2210/pdb1fou/pdb
• Descriptor: UPPER COLLAR PROTEIN (1 entity in total)
• Functional Keywords: alpha-helical barrel, viral protein
• Biological source: Bacillus phage phi29
• Total number of polymer chains: 12
• Total formula weight: 431547.47

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.N.,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

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

Experimental method

X-RAY DIFFRACTION (3.2 Å)