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The crystal structure of Sulfolobus solfataricus elongation factor 1α in complex with GDP reveals novel features in nucleotide binding and exchange
Author(s) -
Vitagliano Luigi,
Masullo Mariorosario,
Sica Filomena,
Zagari Adriana,
Bocchini Vincenzo
Publication year - 2001
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/20.19.5305
Subject(s) - sulfolobus solfataricus , biology , sulfolobus , nucleotide , elongation factor , guanine nucleotide exchange factor , genetics , biochemistry , archaea , gene , signal transduction , rna , ribosome
The crystal structure of elongation factor 1α from the archaeon Sulfolobus solfataricus in complex with GDP ( Ss EF‐1α·GDP) at 1.8 Å resolution is reported. As already known for the eubacterial elongation factor Tu, the Ss EF‐1α·GDP structure consists of three different structural domains. Surprisingly, the analysis of the GDP‐binding site reveals that the nucleotide–protein interactions are not mediated by Mg 2+ . Furthermore, the residues that usually co‐ordinate Mg 2+ through water molecules in the GTP‐binding proteins, though conserved in Ss EF‐1α, are located quite far from the binding site. [ 3 H]GDP binding experiments confirm that Mg 2+ has only a marginal effect on the nucleotide exchange reaction of Ss EF‐1α, although essential to GTPase activity elicited by Ss EF‐1α. Finally, structural comparisons of Ss EF‐ 1α·GDP with yeast EF‐1α in complex with the nucleotide exchange factor EF‐1β shows that a dramatic rearrangement of the overall structure of EF‐1α occurs during the nucleotide exchange.