1ijf
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(New page: 200px<br /><applet load="1ijf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ijf, resolution 3.00Å" /> '''Nucleotide exchange ...)
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Revision as of 15:19, 20 November 2007
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Nucleotide exchange mechanisms in the eEF1A-eEF1Ba complex
Overview
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 Structure
1IJF is a Protein complex structure of sequences from Saccharomyces cerevisiae with MG and G25 as ligands. Full crystallographic information is available from OCA.
Reference
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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