8BAA

CryoEM structure of GroEL-GroES-ADP.AlF3-Rubisco, class II.

This is a non-PDB format compatible entry.

Summary for 8BAA

• Entry DOI: 10.2210/pdb8baa/pdb
• EMDB information: 15944
• Descriptor: Chaperonin GroEL, Co-chaperonin GroES, Ribulose bisphosphate carboxylase, ... (7 entities in total)
• Functional Keywords: groel, groes, chaperone
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 22
• Total formula weight: 932175.15

Authors

Gardner, S.,Saibil, H.R. (deposition date: 2022-10-11, release date: 2025-02-12, Last modification date: 2026-02-25)

Primary citation

Gardner, S.,Darrow, M.C.,Lukoyanova, N.,Thalassinos, K.,Saibil, H.R.
Structural basis of substrate progression through the bacterial chaperonin cycle.
Proc.Natl.Acad.Sci.USA, 120:e2308933120-e2308933120, 2023

PubMed 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·BeF, and GroEL-ADP·AlF-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·BeF to GroEL-Rubisco results in the formation of an intermediate GroEL complex displaying striking asymmetry in the ATP/ADP·BeF-bound ring. In this ring, four GroEL subunits bind Rubisco and the other three are in the GroES-accepting conformation, suggesting how GroEL can recruit GroES without releasing bound substrate. Our cryoEM structures of stalled GroEL-ADP·AlF-Rubisco-GroES complexes show Rubisco folding intermediates interacting with GroEL-GroES via different sets of residues.

PubMed: 38064510
DOI: 10.1073/pnas.2308933120

Experimental method

ELECTRON MICROSCOPY (4.2 Å)