5O8W

CRYSTAL STRUCTURE ANALYSIS OF THE YEAST ELONGATION FACTOR COMPLEX EEF1A:EEF1BA

Summary for 5O8W

• Entry DOI: 10.2210/pdb5o8w/pdb
• Descriptor: Elongation factor 1-alpha, Elongation factor 1-beta, GLUTAMINE, ... (5 entities in total)
• Functional Keywords: protein-protein complex, translation, covalent modification
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 62056.74

Authors

Wirth, C.,Andersen, G.R.,Hunte, C. (deposition date: 2017-06-14, release date: 2017-08-23, Last modification date: 2025-04-09)

Primary citation

Jank, T.,Belyi, Y.,Wirth, C.,Rospert, S.,Hu, Z.,Dengjel, J.,Tzivelekidis, T.,Andersen, G.R.,Hunte, C.,Schlosser, A.,Aktories, K.
Protein glutaminylation is a yeast-specific posttranslational modification of elongation factor 1A.
J. Biol. Chem., 292:16014-16023, 2017

PubMed Abstract: Ribosomal translation factors are fundamental for protein synthesis and highly conserved in all kingdoms of life. The essential eukaryotic elongation factor 1A (eEF1A) delivers aminoacyl tRNAs to the A-site of the translating 80S ribosome. Several studies have revealed that eEF1A is posttranslationally modified. Using MS analysis, site-directed mutagenesis, and X-ray structural data analysis of eEF1A, we identified a posttranslational modification in which the α amino group of mono-l-glutamine is covalently linked to the side chain of glutamate 45 in eEF1A. The MS analysis suggested that all eEF1A molecules are modified by this glutaminylation and that this posttranslational modification occurs at all stages of yeast growth. The mutational studies revealed that this glutaminylation is not essential for the normal functions of eEF1A in However, eEF1A glutaminylation slightly reduced growth under antibiotic-induced translational stress conditions. Moreover, we identified the same posttranslational modification in eEF1A from but not in various other eukaryotic organisms tested despite strict conservation of the Glu residue among these organisms. We therefore conclude that eEF1A glutaminylation is a yeast-specific posttranslational modification that appears to influence protein translation.

PubMed: 28801462
DOI: 10.1074/jbc.M117.801035

Experimental method

X-RAY DIFFRACTION (1.67 Å)