Molecular interactions and residues involved in force generation in the T4 viral DNA packaging motor.

ABSTRACT: Many viruses utilize molecular motors to package their genomes into preformed capsids. A striking feature of these motors is their ability to generate large forces to drive DNA translocation against entropic, electrostatic, and bending forces resisting DNA confinement. A model based on recently resolved structures of the bacteriophage T4 motor protein gp17 suggests that this motor generates large forces by undergoing a conformational change from an extended to a compact state. This transition is proposed to be driven by electrostatic interactions between complementarily charged residues across the interface between the N- and C-terminal domains of gp17. Here we use atomistic molecular dynamics simulations to investigate in detail the molecular interactions and residues involved in such a c

SUBMITTER: Migliori AD 

PROVIDER: S-EPMC4376518 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature