Models for two conformations of the AAA+ chaperone VAT, built into cryo-EM density maps.
Using a combined cryo-EM and solution NMR approach the laboratories of John Rubinstein and Lewis Kay have determined the structure and equilibrium distribution of two unique conformers along the ATP hydrolysis cycle of the AAA+ unfoldase VAT. The paper published in PNAS (http://www.pnas.org/content/113/29/E4190.abstract) lends insight into how this class of molecular machines are able to convert the chemical energy of ATP hydrolysis into the mechanical force required to unfold client proteins. This work was led by Rui Huang and Zev Ripstein.
