7JQP

The Phi-28 gp11 DNA packaging Motor

7JQP の概要

• エントリーDOI: 10.2210/pdb7jqp/pdb
• 関連するPDBエントリー: 7JQ6 7JQ7
• 分子名称: Encapsidation protein, SULFATE ION (3 entities in total)
• 機能のキーワード: atpase, dna packaging, motor, phage, asce fold, viral protein
• 由来する生物種: Lactococcus phage asccphi28
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 225829.59

構造登録者

Morais, M.C.,White, M.A.,Dill, E. (登録日: 2020-08-11, 公開日: 2021-06-16, 最終更新日: 2024-11-06)

主引用文献

Pajak, J.,Dill, E.,Reyes-Aldrete, E.,White, M.A.,Kelch, B.A.,Jardine, P.J.,Arya, G.,Morais, M.C.
Atomistic basis of force generation, translocation, and coordination in a viral genome packaging motor.
Nucleic Acids Res., 49:6474-6488, 2021

PubMed Abstract: Double-stranded DNA viruses package their genomes into pre-assembled capsids using virally-encoded ASCE ATPase ring motors. We present the first atomic-resolution crystal structure of a multimeric ring form of a viral dsDNA packaging motor, the ATPase of the asccφ28 phage, and characterize its atomic-level dynamics via long timescale molecular dynamics simulations. Based on these results, and previous single-molecule data and cryo-EM reconstruction of the homologous φ29 motor, we propose an overall packaging model that is driven by helical-to-planar transitions of the ring motor. These transitions are coordinated by inter-subunit interactions that regulate catalytic and force-generating events. Stepwise ATP binding to individual subunits increase their affinity for the helical DNA phosphate backbone, resulting in distortion away from the planar ring towards a helical configuration, inducing mechanical strain. Subsequent sequential hydrolysis events alleviate the accumulated mechanical strain, allowing a stepwise return of the motor to the planar conformation, translocating DNA in the process. This type of helical-to-planar mechanism could serve as a general framework for ring ATPases.

PubMed: 34050764
DOI: 10.1093/nar/gkab372

実験手法

X-RAY DIFFRACTION (2.89 Å)