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dc.creatorZahn, R. (Ralph)-
dc.creatorBuckle, A.M. (Asley M.)-
dc.creatorPerret, S. (Sarah)-
dc.creatorJohnson, C.M. (Christopher M.)-
dc.creatorCorrales, F.J. (Fernando José)-
dc.creatorGolbik, R. (Ralph)-
dc.creatorFersht, A.R (Alan R.)-
dc.date.accessioned2012-04-03T11:32:36Z-
dc.date.available2012-04-03T11:32:36Z-
dc.date.issued1996-
dc.identifier.citationZahn 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.es_ES
dc.identifier.issn1091-6490-
dc.identifier.urihttp://hdl.handle.net/10171/21566-
dc.description.abstractThe 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.es_ES
dc.language.isoenges_ES
dc.publisherNational Academy of Scienceses_ES
dc.rightsinfo:eu-repo/semantics/openAccesses_ES
dc.subjectAmino Acid Isomerases/chemistryes_ES
dc.subjectCarrier Proteins/chemistryes_ES
dc.subjectChaperonin 60/chemistryes_ES
dc.subjectChaperonin 60/metabolismes_ES
dc.subjectProtein Foldinges_ES
dc.subjectProtein Structure, Secondaryes_ES
dc.titleChaperone activity and structure of monomeric polypeptide binding domains of GroELes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.relation.publisherversionhttp://www.pnas.org/content/93/26/15024es_ES
dc.type.driverinfo:eu-repo/semantics/articlees_ES

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