Structural interplay of the redox co-chaperone CnoX to GroEL/ES chaperonin
Cryo-EM structures reveal how the redox co-chaperone CnoX is accommodated during the GroEL reaction cycle and how GroES binding remodels the apical domains to promote CnoX release. Protein folding by the bacterial chaperonin GroEL/ES relies on ATP-driven conformational cycles that promote substrate encapsulation and fo...