3EZK

Bacteriophage T4 gp17 motor assembly based on crystal structures and cryo-EM reconstructions

3EZK の概要

• エントリーDOI: 10.2210/pdb3ezk/pdb
• 関連するPDBエントリー: 3CPE
• EMDBエントリー: 1572
• 分子名称: DNA packaging protein Gp17 (1 entity in total)
• 機能のキーワード: pentameric motor, dna packaging, alternative initiation, atp-binding, dna-binding, hydrolase, nuclease, nucleotide-binding
• 由来する生物種: Bacteriophage T4
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 331020.31

構造登録者

Sun, S.,Rossmann, M.G. (登録日: 2008-10-23, 公開日: 2009-01-13, 最終更新日: 2023-12-27)

主引用文献

Sun, S.,Kondabagil, K.,Draper, B.,Alam, T.I.,Bowman, V.D.,Zhang, Z.,Hegde, S.,Fokine, A.,Rossmann, M.G.,Rao, V.B.
The structure of the phage T4 DNA packaging motor suggests a mechanism dependent on electrostatic forces.
Cell(Cambridge,Mass.), 135:1251-1262, 2008

PubMed Abstract: Viral genomes are packaged into "procapsids" by powerful molecular motors. We report the crystal structure of the DNA packaging motor protein, gene product 17 (gp17), in bacteriophage T4. The structure consists of an N-terminal ATPase domain, which provides energy for compacting DNA, and a C-terminal nuclease domain, which terminates packaging. We show that another function of the C-terminal domain is to translocate the genome into the procapsid. The two domains are in close contact in the crystal structure, representing a "tensed state." A cryo-electron microscopy reconstruction of the T4 procapsid complexed with gp17 shows that the packaging motor is a pentamer and that the domains within each monomer are spatially separated, representing a "relaxed state." These structures suggest a mechanism, supported by mutational and other data, in which electrostatic forces drive the DNA packaging by alternating between tensed and relaxed states. Similar mechanisms may occur in other molecular motors.

PubMed: 19109896
DOI: 10.1016/j.cell.2008.11.015

実験手法

ELECTRON MICROSCOPY (34 Å)