1F60

CRYSTAL STRUCTURE OF THE YEAST ELONGATION FACTOR COMPLEX EEF1A:EEF1BA

Summary for 1F60

• Entry DOI: 10.2210/pdb1f60/pdb
• Related: 1B64
• Descriptor: ELONGATION FACTOR EEF1A, ELONGATION FACTOR EEF1BA (3 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: 60583.45

Authors

Andersen, G.R.,Pedersen, L.,Valente, L.,Kinzy, T.G.,Nyborg, J. (deposition date: 2000-06-19, release date: 2000-07-04, Last modification date: 2024-02-07)

Primary citation

Andersen, G.R.,Pedersen, L.,Valente, L.,Chatterjee, I.,Kinzy, T.G.,Kjeldgaard, M.,Nyborg, J.
Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha.
Mol.Cell, 6:1261-1266, 2000

PubMed Abstract: The crystal structure of a complex between the protein biosynthesis elongation factor eEF1A (formerly EF-1alpha) and the catalytic C terminus of its exchange factor, eEF1Balpha (formerly EF-1beta), was determined to 1.67 A resolution. One end of the nucleotide exchange factor is buried between the switch 1 and 2 regions of eEF1A and destroys the binding site for the Mg(2+) ion associated with the nucleotide. The second end of eEF1Balpha interacts with domain 2 of eEF1A in the region hypothesized to be involved in the binding of the CCA-aminoacyl end of the tRNA. The competition between eEF1Balpha and aminoacylated tRNA may be a central element in channeling the reactants in eukaryotic protein synthesis. The recognition of eEF1A by eEF1Balpha is very different from that observed in the prokaryotic EF-Tu:EF-Ts complex. Recognition of the switch 2 region in nucleotide exchange is, however, common to the elongation factor complexes and those of Ras:Sos and Arf1:Sec7.

PubMed: 11106763
DOI: 10.1016/S1097-2765(00)00122-2

Experimental method

X-RAY DIFFRACTION (1.67 Å)