1ew4
From Proteopedia
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CRYSTAL STRUCTURE OF ESCHERICHIA COLI CYAY PROTEIN REVEALS A NOVEL FOLD FOR THE FRATAXIN FAMILY
Overview
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, gamma-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-A resolution. It reveals a, protein fold consisting of a six-stranded antiparallel beta-sheet flanked, on one side by two alpha-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.
About this Structure
1EW4 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of Escherichia coli CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family., Cho SJ, Lee MG, Yang JK, Lee JY, Song HK, Suh SW, Proc Natl Acad Sci U S A. 2000 Aug 1;97(16):8932-7. PMID:10908679
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