GroEL

GroEL undergoes R to R" state upon ATP hydrolysis.

K and L helices, the "wing" of apical domain, move downward direction, resulting in the formati...

Upon ATP hydrolysis, GroEL changes its structure from R to R" state. The apical domain rotates more than 100 degree in clockwise manner. As a resul...

Salt bridge (K80-E386) switches to R197-E386 upon ATP binding

Transition of GroEL, a molecular chaperone, from T to R state upon ATP binding. Apical domain including hydrophobic patch (H, I helices) rotates co...