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In the process of protein biosynthesis a crucial role is played by the elongation factor Tu (EF-Tu) in eubacteria and by the elongation factor l α (EF-1a) in eucarya and archaea; it carryies the aa-tRNA to the ribosome, switching from an active GTP bound to an inactive GDP bound form. In the last decade a number of three-dimensional structures of EF-Tu have shed light on the structural details of the elongation cycle in eubacteria. By contrast, very little is known about the structure of the proteins involved in the elongation cycle of eucarya and archaea. Very recently, the 3D structure of the complex of EF-1 α with the C-terminus of EF-1 β from yeast and the structure of EF-1 α from the archaeon Sulfolobus solfataricus in complex with GDP have been reported (1,2). The structure of EF-1 α GDP complex also showed that, in contrast to EFTu, the magnesium (II) ion is not required for the GDP binding whereas it remained essential for the GTPase activity. To further investigate the role of the magnesium in the GDP binding to EF-1 α s, we have also determined the crystal structure of the Sulfolobus solfataricus EF-1 α GDP in the presence of an excess of this ion. The features of magnesium coordination in the refined structure provide clues on the different role played by magnesium in EF-1 α and EF-Tu. References (1)Andersen, G. R.; Pedersen, L.; Valente, L.; Chatterjee, I.; Kinzy, T. G.; Kjeldgaard, M.; Nyborg, J.279(2000) Mol Cell, 6, 1261-1266. (2)Vitagliano, L.; Masullo, M.; Sica, F.; Zagari, A.; Bocchini, V. (2001) Embo J, 20, 5305-5311.

The role of magnesium in the nucleotide binding process ofSulfolobus solfataricuselongation factor 1α