The structural studies of Escherichia coli CyaY at ambient and cryogenic temperatures

Abstract

Abstract Frataxin is a 23 KDa mitochondrial iron-binding protein that is involved in biogenesis of iron-sulfur clusters. A deficiency in frataxin can lead 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 X-ray crystal structure of CyaY protein from Escherichia coli, obtained using the Turkish Light Source “Turkish DeLight”. Furthermore, we determined the cryogenic structure under the same experimental conditions, allowing a detailed comparison between the two structures. This study reveals the structural characteristics of CyaY at near-to-physiological temperature and highlights the importance of temperature dependency in protein structure characterization and providing new insights into protein dynamics.