Ambient temperature crystal structure ofEscherichia coliCyaY protein displays alternate conformation

Abstract

Frataxin is a 23 KDa mitochondrial iron-binding protein that is involved in biogenesis of iron sulfur clusters. A deficiency in frataxin leads to Friedreich's ataxia, a progressive neurodegenerative disorder. The bacterial ortholog of eukaryotic mitochondrial frataxin, CyaY, is thought to play a role in iron sulfur cluster assembly as an iron supplier, making it an important target for study. Here, we present the first ambient temperature crystal structure of CyaY protein from Escherichia coli, obtained using the Turkish Light Source Turkish DeLight. This study reveals the dynamic structural characteristics of CyaY at near-physiological temperature and displays an alternate conformation, highlighting the importance of temperature considerations in protein structure characterization and providing new insights into the protein's flexibility.

Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis

“…Mutations in the sequence and the corresponding loss of function of human frataxin are connected to clinical diseases like Friedreich’s ataxia [33] , [34] , [35] . Meanwhile in Gram-negative bacteria, CyaY, the corresponding protein orthologue to eukaryotic frataxin has been identified for its ability to bind iron and its structural similarity to eukaryotic frataxin and its ability to supply Fe-S cluster proteins with the necessary iron [36] , [37] , [38] . The ability to bind and transfer iron to target recipients (like CpfC) has been shown for a homologous protein in Gram-positive prokaryotic cells, also annotated as frataxin (or protein with an YdhG domain) in Bacillus subtilis .…”