1JNY

Crystal structure of Sulfolobus solfataricus elongation factor 1 alpha in complex with GDP

Summary for 1JNY

• Entry DOI: 10.2210/pdb1jny/pdb
• Descriptor: Elongation factor 1-alpha, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: gtpase, alpha/beta structure, protein biosynthesis, translation
• Biological source: Sulfolobus solfataricus
• Cellular location: Cytoplasm: P35021
• Total number of polymer chains: 2
• Total formula weight: 97964.52

Authors

Vitagliano, L.,Masullo, M.,Sica, F.,Zagari, A.,Bocchini, V. (deposition date: 2001-07-26, release date: 2002-01-23, Last modification date: 2024-02-07)

Primary citation

Vitagliano, L.,Masullo, M.,Sica, F.,Zagari, A.,Bocchini, V.
The crystal structure of Sulfolobus solfataricus elongation factor 1alpha in complex with GDP reveals novel features in nucleotide binding and exchange.
EMBO J., 20:5305-5311, 2001

PubMed Abstract: The crystal structure of elongation factor 1alpha from the archaeon Sulfolobus solfataricus in complex with GDP (SsEF-1alpha.GDP) at 1.8 A resolution is reported. As already known for the eubacterial elongation factor Tu, the SsEF-1alpha.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 SsEF-1alpha, 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 SsEF-1alpha, although essential to GTPase activity elicited by SsEF-1alpha. Finally, structural comparisons of SsEF- 1alpha.GDP with yeast EF-1alpha in complex with the nucleotide exchange factor EF-1beta shows that a dramatic rearrangement of the overall structure of EF-1alpha occurs during the nucleotide exchange.

PubMed: 11574461
DOI: 10.1093/emboj/20.19.5305

Experimental method

X-RAY DIFFRACTION (1.8 Å)