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TitleStructural basis of substrate progression through the bacterial chaperonin cycle.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 120, Issue 50, Page e2308933120, Year 2023
Publish dateDec 12, 2023
AuthorsScott Gardner / Michele C Darrow / Natalya Lukoyanova / Konstantinos Thalassinos / Helen R Saibil /
PubMed AbstractThe 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 ...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.
External linksProc Natl Acad Sci U S A / PubMed:38064510 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 4.4 Å
Structure data

15939

8ba7

EMDB-15939, PDB-8ba7:
CryoEM structure of nucleotide-free GroEL-Rubisco.
Method: EM (single particle) / Resolution: 4.4 Å

15940

8ba8

EMDB-15940, PDB-8ba8:
CryoEM structure of GroEL-ADP.BeF3-Rubisco.
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-15941: CryoEM reconstruction of GroEL-ATP-Rubisco.
Method: EM (single particle) / Resolution: 4.3 Å

15942

8ba9

EMDB-15942, PDB-8ba9:
CryoEM structure of GroEL-GroES-ADP.AlF3-Rubisco.
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-15943: CryoEM reconstruction of GroEL-GroES-ADP.AlF3-Rubisco, class I.
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-15945: CryoEM reconstruction of GroEL-GroES-ADP.AlF3-Rubisco, class III.
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-15946: CryoEM reconstruction of GroEL-GroES-ADP.AlF3-Rubisco, class IV.
Method: EM (single particle) / Resolution: 4.1 Å

Chemicals

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-AF3:
ALUMINUM FLUORIDE

Source
  • escherichia coli (E. coli)
  • escherichia coli k-12 (bacteria)
KeywordsCHAPERONE / GroEL / Rubisco / complex / nucleotide / Chameleon / GroES

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