Conformational shift in the closed state of GroEL induced by ATP-binding triggers a transition to the open state.

ABSTRACT: We investigated the effect of ATP binding to GroEL and elucidated a role of ATP in the conformational change of GroEL. GroEL is a tetradecamer chaperonin that helps protein folding by undergoing a conformational change from a closed state to an open state. This conformational change requires ATP, but does not require the hydrolysis of the ATP. The following three types of conformations are crystalized and the atomic coordinates are available; closed state without ATP, closed state with ATP and open state with ADP. We conducted simulations of the conformational change using Elastic Network Model from the closed state without ATP targeting at the open state, and from the closed state with ATP targeting at the open state. The simulations emphasizing the lowest normal mode showed that the one

SUBMITTER: Suzuki Y 

PROVIDER: S-EPMC5042161 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature