8BA7

CryoEM structure of nucleotide-free GroEL-Rubisco.

This is a non-PDB format compatible entry.

Summary for 8BA7

• Entry DOI: 10.2210/pdb8ba7/pdb
• EMDB information: 15939
• Descriptor: Chaperonin GroEL (1 entity in total)
• Functional Keywords: groel, rubisco, chaperone, complex
• Biological source: Escherichia coli
• Total number of polymer chains: 14
• Total formula weight: 801647.06

Authors

Gardner, S.,Saibil, H.R. (deposition date: 2022-10-11, release date: 2023-10-25, Last modification date: 2023-12-27)

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 (4.4 Å)