1AON

CRYSTAL STRUCTURE OF THE ASYMMETRIC CHAPERONIN COMPLEX GROEL/GROES/(ADP)7

Summary for 1AON

• Entry DOI: 10.2210/pdb1aon/pdb
• Descriptor: GROEL, GROEL/GROES COMPLEX, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: complex (groel-groes), chaperonin assisted protein folding, complex (groel-groes) complex, complex (groel/groes)
• Biological source: Escherichia coli; More
• Total number of polymer chains: 21
• Total formula weight: 877614.16

Authors

Xu, Z.,Horwich, A.L.,Sigler, P.B. (deposition date: 1997-07-08, release date: 1997-10-15, Last modification date: 2024-05-22)

Primary citation

Xu, Z.,Horwich, A.L.,Sigler, P.B.
The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex.
Nature, 388:741-750, 1997

PubMed 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.

PubMed: 9285585
DOI: 10.1038/41944

Experimental method

X-RAY DIFFRACTION (3 Å)