Structural basis of substrate progression through the bacterial chaperonin cycle.

ABSTRACT: The bacterial chaperonin GroEL-GroES promotes protein folding through ATP-regulated cycles of substrate protein binding, encapsulation, and release. Here, we have used cryoEM to determine structures of GroEL, GroEL-ADP·BeF₃, and GroEL-ADP·AlF₃-GroES all complexed with the model substrate Rubisco. Our structures provide a series of snapshots that show how the conformation and interactions of non-native Rubisco change as it proceeds through the GroEL-GroES reaction cycle. We observe specific charged and hydrophobic GroEL residues forming strong initial contacts with non-native Rubisco. Binding of ATP or ADP·BeF₃ to GroEL-Rubisco results in the formation of an intermediate GroEL complex displaying striking asymmetry in the ATP/ADP·BeF₃-bound ring. I

SUBMITTER: Gardner S 

PROVIDER: S-EPMC10723157 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature