Ambient temperature crystal structure ofEscherichia coliCyaY protein displays alternate conformation

Author:

Shafiei AlalehORCID,Baldir NiluferORCID,Na JongbumORCID,Kim Jin HaeORCID,DeMirci HasanORCID

Abstract

AbstractFrataxin 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 fromEscherichia 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.

Publisher

Cold Spring Harbor Laboratory

Cited by 1 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis;Computational and Structural Biotechnology Journal;2023

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