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Dadun > Depósito Académico > CIMA (Centro de Investigación Médica Aplicada) > Área de Terapia génica y Hepatología > Hepatología bioquímica > DA - CIMA - Terapia génica y Hepatología - Hepatología bioquímica - Artículos de revista >

Chaperone activity and structure of monomeric polypeptide binding domains of GroEL
Authors: Zahn, R. (Ralph)
Buckle, A.M. (Asley M.)
Perret, S. (Sarah)
Johnson, C.M. (Christopher M.)
Corrales, F.J. (Fernando José)
Golbik, R. (Ralph)
Fersht, A.R (Alan R.)
Keywords: Amino Acid Isomerases/chemistry
Carrier Proteins/chemistry
Chaperonin 60/chemistry
Chaperonin 60/metabolism
Protein Folding
Protein Structure, Secondary
Issue Date: 1996
Publisher: National Academy of Sciences
Publisher version: http://www.pnas.org/content/93/26/15024
ISSN: 1091-6490
Citation: Zahn R, Buckle AM, Perrett S, Johnson CM, Corrales FJ, Golbik R, et al. Chaperone activity and structure of monomeric polypeptide binding domains of GroEL. Proc Natl Acad Sci U S A 1996 Dec 24;93(26):15024-15029.
Abstract
The chaperonin GroEL is a large complex composed of 14 identical 57-kDa subunits that requires ATP and GroES for some of its activities. We find that a monomeric polypeptide corresponding to residues 191 to 345 has the activity of the tetradecamer both in facilitating the refolding of rhodanese and cyclophilin A in the absence of ATP and in catalyzing the unfolding of native barnase. Its crystal structure, solved at 2.5 A resolution, shows a well-ordered domain with the same fold as in intact GroEL. We have thus isolated the active site of the complex allosteric molecular chaperone, which functions as a "minichaperone." This has mechanistic implications: the presence of a central cavity in the GroEL complex is not essential for those representative activities in vitro, and neither are the allosteric properties. The function of the allosteric behavior on the binding of GroES and ATP must be to regulate the affinity of the protein for its various substrates in vivo, where the cavity may also be required for special functions.
Permanent link: http://hdl.handle.net/10171/21566
Appears in Collections:DA - CIMA - Unidad de Proteómica, Genómica y Bioinformática - Artículos de revista
DA - CIMA - Terapia génica y Hepatología - Hepatología bioquímica - Artículos de revista

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