1FOU

CONNECTOR PROTEIN FROM BACTERIOPHAGE PHI29

1FOU の概要

• エントリーDOI: 10.2210/pdb1fou/pdb
• 分子名称: UPPER COLLAR PROTEIN (1 entity in total)
• 機能のキーワード: alpha-helical barrel, viral protein
• 由来する生物種: Bacillus phage phi29
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 431547.47

構造登録者

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. (登録日: 2000-08-28, 公開日: 2000-12-22, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.2 Å)