Motion in GroEL domain [groeldom]

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Classification Known Domain Motion, Hinge Mechanism [D-h-2]

Structures
1DER Conformation 1 [ PartsList ]
1GRL Conformation 2 [ PartsList ]
1OEL Conformation 3 [ PartsList ]

Description
In marked contrast to the unaffected trans GroEL subunit, the structure of the bound cis GroEL subunit shows profound domain movements. 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. 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.

Particular values describing motion
Location of a Hinge (residue selection) = 137
Location of a Hinge (residue selection) = 410
Location of a Hinge (residue selection) = 192
Location of a Hinge (residue selection) = 375
Experimental Methods = x (Traditional x-ray)
Creation Date = 19971212
Modification Date = 19971212

References
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]

GO terms associated with structures
Molecular functionprotein binding, ATP binding
Biological processcellular protein metabolism

Morphs

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



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