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. 2001 Jun;8(6):531-4.
doi: 10.1038/88598.

Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex

G R Andersen  1 , L Valente, L Pedersen, T G Kinzy, J Nyborg
Affiliations

Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex

G R Andersen et al. Nat Struct Biol. 2001 Jun.

Abstract

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.

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