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Crystal structures of nucleotide exchange intermediates in the eEF1A–eEF1Bα complex


In the elongation cycle of protein biosynthesis, the nucleotide exchange factor eEF1Bα catalyzes the exchange of GDP bound to the G-protein, eEF1A, for GTP. To obtain more information about the recently solved eEF1A–eEF1Bα structure, we determined the structures of the eEF1A–eEF1Bα–GDP–Mg2+, eEF1A–eEF1Bα–GDP and eEF1A–eEF1Bα–GDPNP complexes at 3.0, 2.4 and 2.05 Å resolution, respectively. Minor changes, specifically around the nucleotide binding site, in eEF1A and eEF1Bα are consistent with in vivo data. The base, sugar and α-phosphate bind as in other known nucleotide G-protein complexes, whereas the β- and γ-phosphates are disordered. A mutation of Lys 205 in eEF1Bα 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–eEF1Bα complex.

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Figure 1: Electron densities around the nucleotides after the final refinement.
Figure 2: The exchange mechanism.
Figure 3: The role of Lys 205 in eEF1Bα.

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We are grateful to K. Djinovic at ELETTRA, Trieste, for help during data collection. GRA was supported by Aarhus University. J.N. was supported by the Program for Biotechnological Research of the Danish Natural Science Research Council, DANSYNC, and the EU. T.G.K. was supported by the NIH and the NSF and L.V. by NIH.

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Correspondence to Gregers Rom Andersen.

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Andersen, G., Valente, L., Pedersen, L. et al. Crystal structures of nucleotide exchange intermediates in the eEF1A–eEF1Bα complex. Nat Struct Mol Biol 8, 531–534 (2001).

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