1ije
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Nucleotide Exchange Intermediates in the eEF1A-eEF1Ba Complex
OverviewOverview
In the elongation cycle of protein biosynthesis, the nucleotide exchange, factor eEF1Balpha catalyzes the exchange of GDP bound to the G-protein, eEF1A, for GTP. To obtain more information about the recently solved, eEF1A-eEF1Balpha structure, we determined the structures of the, eEF1A-eEF1Balpha-GDP-Mg2+, eEF1A-eEF1Balpha-GDP and eEF1A-eEF1Balpha-GDPNP, complexes at 3.0, 2.4 and 2.05 A resolution, respectively. Minor changes, specifically around the nucleotide binding site, in eEF1A and eEF1Balpha, are consistent with in vivo data. The base, sugar and alpha-phosphate bind, as in other known nucleotide G-protein complexes, whereas the beta- and, gamma-phosphates are disordered. A mutation of Lys 205 in eEF1Balpha that, inserts into the Mg2+ binding site of eEF1A is lethal. This together with, the structures emphasizes the essential role of Mg2+ in nucleotide, exchange in the eEF1A-eEF1Balpha complex.
About this StructureAbout this Structure
1IJE is a Protein complex structure of sequences from Saccharomyces cerevisiae with G25 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex., Andersen GR, Valente L, Pedersen L, Kinzy TG, Nyborg J, Nat Struct Biol. 2001 Jun;8(6):531-4. PMID:11373622
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