Objective: Eukaryotic translation initiation factor 5A (eIF5A) is a highly conserved protein involved in translation elongation during the synthesis of polyproline motif and require hypusine modification for its activity. Structural differences in eIF5A form eukaryotic pathogens could aid antimicrobial development. This study presents structural data on Candida albicans eIF5A obtained by NMR and X-ray crystallography. Methods: Protein cloning, expression and purification were used for obtaining sample for structural studies and NMR spectroscopy and X-ray crystallography experiments were performed. Results and Discussion: In this work, for the first time, the three-dimensional structure of the eIF5A protein from the pathogenic yeast-like fungus Candida albicans was determined by X-ray crystallography at a resolution of 2.6 Å, and a comparative analysis of the structural data with homologous proteins from S. cerevisiae and H. sapiens was performed. A high degree of conservation in the spatial organization of eIF5A was demonstrated: the mutual arrangement of domains and secondary structure elements is consistent with homologous proteins from other organisms. The obtained structural data are consistent with NMR spectroscopy data and complement the understanding of the spatial organization of proteins of this class. Conclusions: The presented structure of the protein from Candida albicans can serve as a basis for further fundamental studies of its function, as well as for the development of inhibitors targeting enzymes of the hypusination system as a potential target for antifungal therapy.
Gonyalin et al. (2026) studied this question.