Chemical denaturation of the elongation factor 1alpha isolated from the hyperthermophilic archaeon Sulfolobus solfataricus.


Abstract

The stability against chemical denaturants of the elongation factor EF-1alpha (SsEF-1alpha), a protein isolated from the hyperthermophilic archaeon Sulfolobus solfataricus has been characterized in detail. Indeed, the atypical shape of the protein structure and the unusual living conditions of the host organism prompted us to analyze the effect of urea and guanidine hydrochloride (GuHCl) on the GDP complex of the enzyme (SsEF-1alpha x GDP) by fluorescence and circular dichroism. These studies were also extended to the nucleotide-free form of the protein (nfSsEF-1alpha). Interestingly, the experiments show that the denaturation curves of both SsEF-1alpha forms present a single inflection point, which is indicative of a cooperative unfolding process with no intermediate species. Moreover, the chemically induced unfolding process of both SsEF-1alpha x GDP and nfSsEF-1alpha is fully reversible. Both SsEF-1alpha forms exhibit remarkable stability against urea, but they do not display a strong resistance to the denaturing action of GuHCl. These findings suggest that electrostatic interactions significantly contribute to SsEF-1alpha stability. Study holds ProTherm entries: 19757, 19758, 19759, 19760, 19761, 19762, 19763, 19764, 19765, 19766, 19767, 19768, 19769, 19770, 19771, 19772, 19773, 19774, 19775, 19776 Extra Details: hyperthermophilic archaeon; nucleotide-free form; cooperative unfolding; electrostatic interactions

Submission Details

ID: QGmCPLPw

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:52 p.m.

Version: 1

Publication Details
Granata V;Graziano G;Ruggiero A;Raimo G;Masullo M;Arcari P;Vitagliano L;Zagari A,Biochemistry (2006) Chemical denaturation of the elongation factor 1alpha isolated from the hyperthermophilic archaeon Sulfolobus solfataricus. PMID:16411747
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
1SKQ 2004-07-20 1.8 The crystal structure of Sulfolobus solfataricus elongation factor 1-alpha in complex with magnesium and GDP
1JNY 2002-01-23 1.8 Crystal structure of Sulfolobus solfataricus elongation factor 1 alpha in complex with GDP

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Elongation factor 1-alpha P35021 EF1A_SACS2