The Structure of the Phage T4 DNA Packaging Motor Suggests a Mechanism Dependent on Electrostatic Forces
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.
- Authors:
-
- CUA
- Publication Date:
- Research Org.:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1007116
- Resource Type:
- Journal Article
- Journal Name:
- Cell
- Additional Journal Information:
- Journal Volume: 135; Journal Issue: (7) ; 12, 2008; Journal ID: ISSN 0092-8674
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 36 MATERIALS SCIENCE; BACTERIOPHAGES; COMPACTING; CRYSTAL STRUCTURE; DNA; ELECTROSTATICS; GENES; MICROSCOPY; MONOMERS; MOTORS; NUCLEASES; PACKAGING
Citation Formats
Sun, Siyang, Kondabagil, Kiran, Draper, Bonnie, Alam, Tanfis I, Bowman, Valorie D, Zhang, Zhihong, Hegde, Shylaja, Fokine, Andrei, Rossmann, Michael G, Rao, Venigalla B, and Purdue). The Structure of the Phage T4 DNA Packaging Motor Suggests a Mechanism Dependent on Electrostatic Forces. United States: N. p., 2009.
Web. doi:10.1016/j.cell.2008.11.015.
Sun, Siyang, Kondabagil, Kiran, Draper, Bonnie, Alam, Tanfis I, Bowman, Valorie D, Zhang, Zhihong, Hegde, Shylaja, Fokine, Andrei, Rossmann, Michael G, Rao, Venigalla B, & Purdue). The Structure of the Phage T4 DNA Packaging Motor Suggests a Mechanism Dependent on Electrostatic Forces. United States. https://doi.org/10.1016/j.cell.2008.11.015
Sun, Siyang, Kondabagil, Kiran, Draper, Bonnie, Alam, Tanfis I, Bowman, Valorie D, Zhang, Zhihong, Hegde, Shylaja, Fokine, Andrei, Rossmann, Michael G, Rao, Venigalla B, and Purdue). 2009.
"The Structure of the Phage T4 DNA Packaging Motor Suggests a Mechanism Dependent on Electrostatic Forces". United States. https://doi.org/10.1016/j.cell.2008.11.015.
@article{osti_1007116,
title = {The Structure of the Phage T4 DNA Packaging Motor Suggests a Mechanism Dependent on Electrostatic Forces},
author = {Sun, Siyang and Kondabagil, Kiran and Draper, Bonnie and Alam, Tanfis I and Bowman, Valorie D and Zhang, Zhihong and Hegde, Shylaja and Fokine, Andrei and Rossmann, Michael G and Rao, Venigalla B and Purdue)},
abstractNote = {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.},
doi = {10.1016/j.cell.2008.11.015},
url = {https://www.osti.gov/biblio/1007116},
journal = {Cell},
issn = {0092-8674},
number = (7) ; 12, 2008,
volume = 135,
place = {United States},
year = {Tue Jun 30 00:00:00 EDT 2009},
month = {Tue Jun 30 00:00:00 EDT 2009}
}