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Conformational Changes In GROEL Induced by a Protein Substrate

Published online by Cambridge University Press:  02 July 2020

S. Falke ,
M. Fisher  and
E. Gogol
S. Falke
Affiliation:
Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS66160.
M. Fisher
Affiliation:
Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS66160.
E. Gogol
Affiliation:
School of Biological Sciences, University of Missouri-Kansas City, Kansas City, MO64110.
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Extract

The GroEL/GroES chaperonin system of E. coli facilitates nucleotide dependent folding of select proteins. The structure of GroEL has been described by three-dimensional electron microscopy and at higher resolution by X-ray crystallography. The GroEL oligomer is a cylindrical tetradecamer composed of two heptameric rings of 57 kDa protein subunits, stacked back to back. Each subunit is comprised of two large domains, equatorial and apical, connected by a smaller intermediate domain. The intermediate “hinge” domain links the apical and equatorial domain and provides flexibility for en bloc rearrangement associated with nucleotide and GroES binding. Equatorial domains are responsible for interactions between the two heptamers and contain the ATPase activity of GroEL. Each ring of GroEL has a central cavity that is the binding site for denatured protein substrate. GroES and denatured substrate binding sites are located on the apical domains facing the central cavity.

Type
Electron Cryomicroscopy of Macromolecules
Information
Microscopy and Microanalysis , Volume 6 , Issue S2: Proceedings: Microscopy & Microanalysis 2000, Microscopy Society of America 58th Annual Meeting, Microbeam Analysis Society 34th Annual Meeting, Microscopical Society of Canada/Societe de Microscopie de Canada 27th Annual Meeting, Philadelphia, Pennsylvania August 13-17, 2000 , August 2000 , pp. 258 - 259
Copyright
Copyright © Microscopy Society of America

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References

1.Fenton, W. A., and Horwich, A. L.Protein Science 6, (1997) 743.CrossRefGoogle Scholar
2.Chen, S. et al. Nature, 371 (1994)261.CrossRefGoogle Scholar
3.Xu, Z., Horwich, A. L., and Sigler, P. B.Nature 388, (1997) 741.CrossRefGoogle Scholar
4.Fisher, M. T.Biochemistry 31, (1992) 3955.CrossRefGoogle Scholar