Shelley Grimes

TL;DR: The force–velocity relationship of the motor is established and it is found that the rate-limiting step of the machine's cycle is force dependent even at low loads, suggesting that this force may be available for initiating the ejection of the DNA from the capsid during infection.

TL;DR: In this article, the structure of the head-tail connector of the Bacillus subtilis bacteriophage phi29 was determined by means of X-ray crystallography, and the connector was fitted into the electron densities of the prohead and of the partially packaged prohead.

TL;DR: The kinetic parameters of the packaging motor and their dependence on external load are determined to show that DNA translocation does not occur during ATP binding but is likely triggered by phosphate release, and a minimal mechanochemical cycle of this DNA-translocating ATPase is proposed.

TL;DR: The direct observation of the intersubunit coordination and step size of a ring ATPase, the double-stranded-DNA packaging motor in the bacteriophage ϕ29, indicates that the hydrolysis cycles of the individual subunits are highly coordinated by means of a mechanism novel for ring ATPases.

TL;DR: The force-velocity relationship of the motor is established and it is found that the rate-limiting step of the machine's cycle is force dependent even at low loads, suggesting that this force may be available for initiating the ejection of the DNA from the capsid during infection.