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dc.contributor.authorPozo Dengra, Joaquín 
dc.contributor.authorMartínez Rodríguez, Sergio 
dc.contributor.authorContreras Moyeja, Lellys Mariela 
dc.contributor.authorPrieto, J
dc.contributor.authorAndújar Sánchez, Montserrat 
dc.contributor.authorClemente Jiménez, Josefa María 
dc.contributor.authorLas Heras Vázquez, Francisco Javier 
dc.contributor.authorRodríguez Vico, Felipe 
dc.contributor.authorNeira Faleiro, José Luis 
dc.date.accessioned2024-05-22T09:46:51Z
dc.date.available2024-05-22T09:46:51Z
dc.date.issued2009
dc.identifier.issn0006-3525
dc.identifier.urihttp://hdl.handle.net/10835/16526
dc.description.abstractThe N-succinylamino acid racemases (NSAAR) belong to the enolase superfamily and they are large homooctameric/hexameric species that require a divalent metal ion for activity. We describe the structure and stability of NSAAR from Geobacillus kaustophilus (GkNSAAR) in the absence and in the presence of Co21 by using hydrodynamic and spectroscopic techniques. The Co21, among other assayed divalent ions, provides the maximal enzymatic activity at physiological pH. The protein seems to be a tetramer with a rather elongated shape, as shown by AU experiments; this is further supported by the modeled structure, which keeps intact the largest tetrameric oligomerization interfaces observed in other homooctameric members of the family, but it does not maintain the octameric oligomerization interfaces. The native functional structure is mainly formed by ahelix, as suggested by FTIR and CD deconvoluted spectra, with similar percentages of structure to those observed in other protomers of the enolase superfamily. At low pH, the protein populates a molten-globule-like conformation. The GdmCl denaturation occurs through a monomeric intermediate, and thermal denaturation experiments indicate a high thermostability. The presence of the cofactor Co21 did alter slightly the secondary structure, but it did not modify substantially the stability of the protein. Thus, GkNSAAR is one of the few members of the enolase family whose conformational propensities and stability have been extensively characterized.es_ES
dc.language.isoenes_ES
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectN-succinylamino acid racemasees_ES
dc.subjectprotein stabilityes_ES
dc.subjectprotein structurees_ES
dc.subjecttetrameres_ES
dc.subjectfluorescencees_ES
dc.subjectenolase superfamilyes_ES
dc.titleStructure and Conformational Stability of a Tetrameric Thermostable N-Succinylamino Acid Racemasees_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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Attribution-NonCommercial-NoDerivatives 4.0 Internacional
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