3P9A

An atomic view of the nonameric small terminase subunit of Bacteriophage P22

3P9A の概要

• エントリーDOI: 10.2210/pdb3p9a/pdb
• 分子名称: DNA-packaging protein gp3 (2 entities in total)
• 機能のキーワード: terminase small subunit, dna packaging, bacteriophage p22, dna binding protein
• 由来する生物種: Enterobacteria phage P22 (Bacteriophage P22)
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 168075.44

構造登録者

Bhardwaj, A.,Roy, A.,Cingolani, G. (登録日: 2010-10-17, 公開日: 2012-05-09, 最終更新日: 2024-02-21)

主引用文献

Roy, A.,Bhardwaj, A.,Datta, P.,Lander, G.C.,Cingolani, G.
Small terminase couples viral DNA binding to genome-packaging ATPase activity.
Structure, 20:1403-1413, 2012

PubMed Abstract: Packaging of viral genomes into empty procapsids is powered by a large DNA-packaging motor. In most viruses, this machine is composed of a large (L) and a small (S) terminase subunit complexed with a dodecamer of portal protein. Here we describe the 1.75 Å crystal structure of the bacteriophage P22 S-terminase in a nonameric conformation. The structure presents a central channel ∼23 Å in diameter, sufficiently large to accommodate hydrated B-DNA. The last 23 residues of S-terminase are essential for binding to DNA and assembly to L-terminase. Upon binding to its own DNA, S-terminase functions as a specific activator of L-terminase ATPase activity. The DNA-dependent stimulation of ATPase activity thus rationalizes the exclusive specificity of genome-packaging motors for viral DNA in the crowd of host DNA, ensuring fidelity of packaging and avoiding wasteful ATP hydrolysis. This posits a model for DNA-dependent activation of genome-packaging motors of general interest in virology.

PubMed: 22771211
DOI: 10.1016/j.str.2012.05.014

実験手法

X-RAY DIFFRACTION (1.755 Å)