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| [[Image:1jny.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1jny| PDB=1jny | SCENE= }} | | {{STRUCTURE_1jny| PDB=1jny | SCENE= }} |
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| '''Crystal structure of Sulfolobus solfataricus elongation factor 1 alpha in complex with GDP'''
| | ===Crystal structure of Sulfolobus solfataricus elongation factor 1 alpha in complex with GDP=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_11574461}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11574461 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11574461}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Gtpase]] | | [[Category: Gtpase]] |
| [[Category: Protein biosynthesis]] | | [[Category: Protein biosynthesis]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:28:49 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:32:03 2008'' |