1G7C

YEAST EEF1A:EEF1BA IN COMPLEX WITH GDPNP

Summary for 1G7C

• Entry DOI: 10.2210/pdb1g7c/pdb
• Related: 1F60
• Descriptor: ELONGATION FACTOR 1-ALPHA, ELONGATION FACTOR 1-BETA, GUANOSINE-5'-MONOPHOSPHATE, ... (4 entities in total)
• Functional Keywords: protein-protein complex, translation
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Cytoplasm: P02994
• Total number of polymer chains: 2
• Total formula weight: 60946.67

Authors

Andersen, G.R.,Valente, L.,Pedersen, L.,Kinzy, T.G.,Nyborg, J. (deposition date: 2000-11-10, release date: 2000-12-06, Last modification date: 2023-08-09)

Primary citation

Andersen, G.R.,Valente, L.,Pedersen, L.,Kinzy, T.G.,Nyborg, J.
Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex.
Nat.Struct.Biol., 8:531-534, 2001

PubMed 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.

PubMed: 11373622
DOI: 10.1038/88598

Experimental method

X-RAY DIFFRACTION (2.05 Å)