Article
Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 Å resolution.
Proceedings of the National Academy of Sciences of the United States of America - 6 Aug 2013
Fei Xue, Yang Dong, LaRonde-LeBlanc Nicole, Lorimer George H
Abstract excerpt
The chaperonin proteins GroEL and GroES are cellular nanomachines driven by the hydrolysis of ATP that facilitate the folding of structurally diverse substrate proteins. In response to ligand binding, the subunits of a ring cycle in a concerted manner through a series of allosteric states (T, R, and R″), enabling work to be performed on the substrate protein. Removing two salt bridges that ordinarily break during...
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