Motion in GroEL [groel]

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Classification Complex Motion [C----]

1AON Conformation 1 [ PartsList ]
1DER Conformation 2 [ PartsList ]
1GRL Conformation 3 [ PartsList ]
1OEL Conformation 4 [ PartsList ]

Chaperonins enhance protein folding with the consumption of ATP. They exist as multi-subunit protein assemblies comprising rings of subunits stacked back to back. The recent crystallographic structure of GroEL-GroES-(ADP)7. (Xu et al., 1997) show that both subunit and domain motions are involved in the operation of the GroEl chaperone. The cis ring intermediate and apical domains engage in large enbloc movements and thereby enable bound GroES to stabilize a folding chamber with ADP confined to the cis ring. The apical domains twist and elevate, doubling the volume of the central cavity and burying hydrophobic residues in the interface with GroES, as well as between GroEL subunits. This leaves 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.
In marked contrast to the unaffected trans GroEL subunit, the structure of the bound cis GroEL subunit shows profound differences, which Xu et al. attribute to dramatic domain rearrangements involving both the intermediate and apical domains. The intermediate domain swings down towards the equatorial domain and the central channel, pivoting approximately 25 degrees around Pro 137 and Gly410, which form a slender link to the equatorial domain. The movement closes the nucleotide-binding site that is located on the top inner surface of the equatorial domain, both within the same subunit and with a neighboring subunit. Their interactions seem sterically to impede the dissociation of ADP from the cis ring, and they structurally relate GroES binding to the presence of ATP and to ATP hydrolysis in the cis ring. Second, the apical domain swings up 60 degrees relative to the equator and twists around the long axis of the domain by about 90 degrees, leading to an interaction with mobile loop of GroES. The pivot point of the apical movement is again a slender link, in this case a pair of Gly residues (Gly 192 and Gly 375) between the intermediate and apical domains, which links the position of the apical domain to the nucleotide-induced/stabilized movement of the intermediate domain. The movement of the hinge in response to nucleotide directly couples the binding of GroES to the presence of the nucleotide, and vice versa. Both domain movements (intermediate and apical) are largely en bloc, with RMS deviations for superposition of these domains upon their unliganded counterparts of 0.91 and 1.66 A for the intermediate and apical domains, respectively. These domain movements, especially in the apical domains, dramatically rearrange the cavity formed by the cis GroEL ring and GroES. The volume of the cavity is doubled, and the polypeptide binding properties of the cavity lining are changed.

Particular values describing motion
Creation Date = 19971130
Experimental Methods = x (Traditional x-ray)
Location of a Hinge (residue selection) = 137
Location of a Hinge (residue selection) = 192
Location of a Hinge (residue selection) = 375
Location of a Hinge (residue selection) = 410
Modification Date = 1999-05-24 16:38:41.000

K Braig, Z Otwinowski, R Hegde, D C Boisvert, A Joachimiak, A L Horwich and P B Sigler (1994). The crystal structure of the bacterial chaperonin GroEL at 2.8 A [see comments]. Nature. 371: 578-586. [Medline info for 95021709]
Rye HS, Burston SG, Fenton WA, Beechem JM, Xu Z, Sigler PB, Horwich AL (1997). Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature 388(6644):792-798. [Medline info for 97429955]
Xu Z, Horwich AL, Sigler PB (1997). The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388(6644):741-750. [Medline info for 97429947]

Data and Graphics
Custom movies Morph of entire double ring of GroEL (1AON->1DER). Several movies and structure files available.

GO terms associated with structures
Molecular functionprotein binding, ATP binding
Biological processprotein folding, cellular protein metabolism


[ show all images ]
Best representative
Morph Morph name Structure #1 Structure #2 Residues
GroEL 1aon [ A ] 1oel [ A ] 547

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
479788-30991 CryoEM structure of GroEL 1gr5 [ ] 1gr6 [ ] 517
06009-14191 GroEl 1oel [ A ] 1aon [ A ] 547
09094-23971 GroEL 1oel [ A ] 1aon [ A ] 547
09113-24041 GroEL 1oel [ A ] 1aon [ A ] 547
70728-14400 GroEL 1grl [ A ] 1oel [ A ] 547
71095-15408 GroEL 1aon [ A ] 1oel [ A ] 547
794567-20417 GroEL 1aon [ A ] 1oel [ A ] 547
groel GroEL 1grl [ ] file2 [ ] 548
341168-2858 GroEL upload [ A ] upload [ A ] 547
342369-3428 GroEL upload [ A ] upload [ A ] 547
868140-1949 GroEL upload [ A ] upload [ A ] 525
698917-12685 GroEL 1oel [ A ] 1kp8 [ A ] 547
758521-19057 GroEL 1oel [ A ] 1aon [ A ] 547
424468-21563 GroEL (1GR5/1GR6: Chain A) upload [ A ] upload [ A ] 547
402535-16940 GroEL (A chain) upload [ A ] upload [ A ] 547
374287-21991 GroEL from E. coli upload [ J ] upload [ D ] 547
143328-11432 GroEL Subunit upload [ N ] upload [ A ] 524
690520-2332 GroEL subunit A upload [ A ] upload [ A ] 524
731010-1033 GroEL subunit A upload [ A ] upload [ A ] 524

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_