Structure and Conformational Stability of a Tetrameric Thermostable N-Succinylamino Acid Racemase
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Pozo Dengra, Joaquín; Martínez Rodríguez, Sergio; Contreras Moyeja, Lellys Mariela; Prieto, J; Andújar Sánchez, Montserrat; [et al.]Fecha
2009Resumen
The 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 e...
Palabra/s clave
N-succinylamino acid racemase
protein stability
protein structure
tetramer
fluorescence
enolase superfamily