According to the binding-zipper model, the RecA class of ATPase motors converts chemical energy into mechanical force by the progressive annealing of hydrogen bonds between the nucleotide and the catalytic pocket. The role of hydrolysis is to weaken the binding of products, allowing them to be released so that the cycle can repeat. Molecular dynamics can be used to study the unbinding process, but the binding process is more complex, so that inferences about it are made indirectly from structural, mutation, and biochemical studies. Here we present a series of models of varying complexity that illustrate the basic processes involved in force production during ATP binding. These models reveal the role of solvent and geometry in determining the amount of mechanical work that can be extracted from the binding process.
|Number of pages||14|
|State||Published - Jun 2006|
Bibliographical noteFunding Information:
J.E. and A.C. were supported by the National Science Foundation and Defense Advanced Research Projects Agency. G.O. was supported by National Institutes of Health grant No. GM59875-02.