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7CNB

Crystal structure of Gp16 C-terminal domain from Bacillus virus phi29

7CNB の概要
エントリーDOI10.2210/pdb7cnb/pdb
分子名称DNA packaging protein (1 entity in total)
機能のキーワードcrystal structure of gp16 c-terminal domain from bacillus virus phi29, motor protein
由来する生物種Bacillus phage phi29
タンパク質・核酸の鎖数1
化学式量合計12675.44
構造登録者
Ouyang, S.Y.,Saeed, A.F.U.H. (登録日: 2020-07-30, 公開日: 2021-03-24, 最終更新日: 2024-03-27)
主引用文献Saeed, A.F.U.H.,Chan, C.,Guan, H.,Gong, B.,Guo, P.,Cheng, X.,Ouyang, S.
Structural Insights into gp16 ATPase in the Bacteriophage φ29 DNA Packaging Motor.
Biochemistry, 60:886-897, 2021
Cited by
PubMed Abstract: Biological motors, ubiquitous in living systems, convert chemical energy into different kinds of mechanical motions critical to cellular functions. Gene product 16 (gp16) in bacteriophage ϕ29 is among the most powerful biomotors known, which adopts a multisubunit ring-shaped structure and hydrolyzes ATP to package double-stranded DNA (dsDNA) into a preformed procapsid. Here we report the crystal structure of the C-terminal domain of gp16 (gp16-CTD). Structure-based alignment and molecular dynamics simulations revealed an essential binding surface of gp16-CTD for prohead RNA, a unique component of the motor complex. Furthermore, our simulations highlighted a dynamic interplay between the N-terminal domain and the CTD of gp16, which may play a role in driving movement of DNA into the procapsid. Lastly, we assembled an atomic structural model of the complete ϕ29 dsDNA packaging motor complex by integrating structural and experimental data from multiple sources. Collectively, our findings provided a refined inchworm-revolution model for dsDNA translocation in bacteriophage ϕ29 and suggested how the individual domains of gp16 work together to power such translocation.
PubMed: 33689296
DOI: 10.1021/acs.biochem.0c00935
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.32 Å)
構造検証レポート
Validation report summary of 7cnb
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-04-09に公開中

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