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The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex.
Nature. 1997 Aug 21; 388(6644):741-50.Nat

Abstract

Chaperonins assist protein folding with the consumption of ATP. They exist as multi-subunit protein assemblies comprising rings of subunits stacked back to back. In Escherichia coli, asymmetric intermediates of GroEL are formed with the co-chaperonin GroES and nucleotides bound only to one of the seven-subunit rings (the cis ring) and not to the opposing ring (the trans ring). The structure of the GroEL-GroES-(ADP)7 complex reveals how large en bloc movements of the cis ring's intermediate and apical domains enable bound GroES to stabilize a folding chamber with ADP confined to the cis ring. Elevation and twist of the apical domains double the volume of the central cavity and bury hydrophobic peptide-binding residues in the interface with GroES, as well as between GroEL subunits, leaving a hydrophilic cavity lining that is conducive to protein folding. An inward tilt of the cis equatorial domain causes an outward tilt in the trans ring that opposes the binding of a second GroES. When combined with new functional results, this negative allosteric mechanism suggests a model for an ATP-driven folding cycle that requires a double toroid.

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Authors+Show Affiliations

Xu Z
The Howard Hughes Medical Institute, The Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510, USA.
Horwich AL
No affiliation info available
Sigler PB
No affiliation info available

MeSH

Adenosine DiphosphateAllosteric RegulationAmino Acid SequenceBinding SitesChaperonin 10Chaperonin 60Crystallography, X-RayEscherichia coliMacromolecular SubstancesModels, MolecularMolecular Sequence DataProtein ConformationProtein FoldingRecombinant Proteins

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

9285585

Citation

Xu, Z, et al. "The Crystal Structure of the Asymmetric GroEL-GroES-(ADP)7 Chaperonin Complex." Nature, vol. 388, no. 6644, 1997, pp. 741-50.
Xu Z, Horwich AL, Sigler PB. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature. 1997;388(6644):741-50.
Xu, Z., Horwich, A. L., & Sigler, P. B. (1997). The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature, 388(6644), 741-50.
Xu Z, Horwich AL, Sigler PB. The Crystal Structure of the Asymmetric GroEL-GroES-(ADP)7 Chaperonin Complex. Nature. 1997 Aug 21;388(6644):741-50. PubMed PMID: 9285585.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. AU - Xu,Z, AU - Horwich,A L, AU - Sigler,P B, PY - 1997/8/21/pubmed PY - 2001/3/23/medline PY - 1997/8/21/entrez SP - 741 EP - 50 JF - Nature JO - Nature VL - 388 IS - 6644 N2 - Chaperonins assist protein folding with the consumption of ATP. They exist as multi-subunit protein assemblies comprising rings of subunits stacked back to back. In Escherichia coli, asymmetric intermediates of GroEL are formed with the co-chaperonin GroES and nucleotides bound only to one of the seven-subunit rings (the cis ring) and not to the opposing ring (the trans ring). The structure of the GroEL-GroES-(ADP)7 complex reveals how large en bloc movements of the cis ring's intermediate and apical domains enable bound GroES to stabilize a folding chamber with ADP confined to the cis ring. Elevation and twist of the apical domains double the volume of the central cavity and bury hydrophobic peptide-binding residues in the interface with GroES, as well as between GroEL subunits, leaving a hydrophilic cavity lining that is conducive to protein folding. An inward tilt of the cis equatorial domain causes an outward tilt in the trans ring that opposes the binding of a second GroES. When combined with new functional results, this negative allosteric mechanism suggests a model for an ATP-driven folding cycle that requires a double toroid. SN - 0028-0836 UR - https://www.unboundmedicine.com/medline/citation/9285585/The_crystal_structure_of_the_asymmetric_GroEL_GroES__ADP_7_chaperonin_complex_ L2 - https://doi.org/10.1038/41944 DB - PRIME DP - Unbound Medicine ER -