PMID:9285585
| Citation |
Xu, Z, Horwich, AL and Sigler, PB (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388:741-50 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1038/41944 |
| Keywords |
Adenosine Diphosphate/chemistry; Allosteric Regulation; Amino Acid Sequence; Binding Sites; Chaperonin 10/chemistry; Chaperonin 10/genetics; Chaperonin 60/chemistry; Chaperonin 60/genetics; Crystallography, X-Ray; Escherichia coli; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Folding; Recombinant Proteins/chemistry; Recombinant Proteins/genetics |
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