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Crystal structure of Escherichia coli CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family

By Seung-Je Cho, Myong Gyong Lee, Jin Kuk Yang, Jae Young Lee, Hyun Kyu Song and Se Won Suh

Abstract

Friedreich ataxia is an autosomal recessive neurodegenerative disease caused by defects in the FRDA gene, which encodes a mitochondrial protein called frataxin. Frataxin is evolutionarily conserved, with homologs identified in mammals, worms, yeast, and bacteria. The CyaY proteins of γ-purple bacteria are believed to be closely related to the ancestor of frataxin. In this study, we have determined the crystal structure of the CyaY protein from Escherichia coli at 1.4-Å resolution. It reveals a protein fold consisting of a six-stranded antiparallel β-sheet flanked on one side by two α-helices. This fold is likely to be shared by all members of the conserved frataxin family. This study also provides a framework for the interpretation of disease-associated mutations in frataxin and for understanding the possible functions of this protein family

Topics: Biological Sciences
Publisher: The National Academy of Sciences
Year: 2000
OAI identifier: oai:pubmedcentral.nih.gov:16799
Provided by: PubMed Central
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