GroEL "relaxed" conformation
One end of GroEL is transiently blocked by the co-chaperonin GroES, an assembly of 10,000-MW subunits. (b) In the absence of ATP or presence of ADP GroEL exists in a "tight" conformational state that binds partly folded or misfolded proteins. Binding of ATP shifts GroEL to a more open, "relaxed" state, which releases the folded protein. See text for details. [Part (b) from A. Roseman et al., 1996, Cell 87:241; courtesy of H. Saibil.]
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