title: A charged performance by gp17 in viral packaging.
abstract: Packaging of viral genomes into virus capsids requires powerful motors to overcome the repulsive force that builds as the nucleic acids are compressed. Through structural analyses of the T4 bacteriophage packaging motor gp17, Sun et al. (2008) now propose a packaging mechanism in which electrostatic forces cause the motor to alternate between tensed and relaxed conformational states.
authors.affiliation: The Scripps Research Institute, The Skaggs Institute for Chemical Biology, La Jolla, CA 92037, USA.
authors.forename: R Scott
authors.initials: RS
authors.lastname: Williams
authors.forename: Gareth J
authors.initials: GJ
authors.lastname: Williams
authors.forename: John A
authors.initials: JA
authors.lastname: Tainer
mesh_terms: D017122:Bacteriophage T4 / Q000378:metabolism*; D042003:DNA Packaging; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism*; D019065:Virus Assembly
chemical_list: D014764:Viral Proteins; C065038:gp17 protein, Enterobacteria phage T4