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J. Biol. Chem., Vol. 277, Issue 46, 44050-44060, November 15, 2002

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SDS-resistant Active and Thermostable Dimers Are Obtained from the Dissociation of Homotetrameric -Glycosidase from Hyperthermophilic Sulfolobus solfataricus in SDS
STABILIZING ROLE OF THE A-C INTERMONOMERIC INTERFACE^*

Fabrizio Gentile, Pietro Amodeo^§, Ferdinando Febbraio^¶, Francesco Picaro, Andrea Motta^§, Silvestro Formisano, and Roberto Nucci^¶

From the  Istituto di Endocrinologia e Oncologia Sperimentale del CNR and Dipartimento di Biologia e Patologia Cellulare e Molecolare, Università Federico II, Via Pansini 5, 80131 Napoli, ^§ Istituto di Chimica Biomolecolare del CNR, Via Campi Flegrei 34, 80078 Pozzvoli, Napoli, and ^¶ Istituto di Biochimica delle Proteine del CNR, Via Marconi 10, 80125 Napoli, Italy

-Glycosidases are fundamental, widely conserved enzymes. Those from hyperthermophiles exhibit unusual stabilities toward various perturbants. Previous work with homotetrameric -glycosidase from hyperthermophilic Sulfolobus solfataricus (M_r 226,760) has shown that addition of 0.05-0.1% SDS was associated with minimal secondary structure perturbations and increased activity. This work addresses the effects of SDS on -glycosidase quaternary structure. In 0.1-1% SDS, the enzyme was dimeric, as determined by Ferguson analysis of transverse-gradient polyacrylamide gels. The catalytic activity of the -glycosidase dimer in SDS was determined by in-gel assay. A minor decrease of thermal stability in SDS was observed after exposure to temperatures up to 80 °C for 1 h. An analysis of -glycosidase crystal structure showed different changes in solvent-accessible surface area on going from the tetramer to the two possible dimers (A-C and A-D). Energy minimization and molecular dynamics calculations showed that the A-C dimer, exhibiting the lowest exposed surface area, was more stabilized by a network of polar interactions. The charge distribution around the A-C interface was characterized by a local short range anisotropy, resulting in an unfavorable interaction with SDS. This paper provides a detailed description of an SDS-resistant inter-monomeric interface, which may help understand similar interfaces involved in important biological processes.

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