The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex - PubMed (original) (raw)
. 1997 Aug 21;388(6644):741-50.
doi: 10.1038/41944.
Affiliations
- PMID: 9285585
- DOI: 10.1038/41944
The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
Z Xu et al. Nature. 1997.
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.
Comment in
- Protein folding. Folding with a two-stroke motor.
Lorimer G. Lorimer G. Nature. 1997 Aug 21;388(6644):720-1, 723. doi: 10.1038/41892. Nature. 1997. PMID: 9285577 No abstract available.
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