1EW4
CRYSTAL STRUCTURE OF ESCHERICHIA COLI CYAY PROTEIN REVEALS A NOVEL FOLD FOR THE FRATAXIN FAMILY
Summary for 1EW4
| Entry DOI | 10.2210/pdb1ew4/pdb |
| Descriptor | CYAY PROTEIN (2 entities in total) |
| Functional Keywords | friedreich ataxia, frataxin family, cyay, iron homeostasis, unknown function |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 12242.36 |
| Authors | Suh, S.W.,Cho, S.,Lee, M.G.,Yang, J.K.,Lee, J.Y.,Song, H.K. (deposition date: 2000-04-22, release date: 2000-08-09, Last modification date: 2024-02-07) |
| Primary citation | Cho, S.J.,Lee, M.G.,Yang, J.K.,Lee, J.Y.,Song, H.K.,Suh, S.W. Crystal structure of Escherichia coli CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family. Proc.Natl.Acad.Sci.USA, 97:8932-8937, 2000 Cited by PubMed 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 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. PubMed: 10908679DOI: 10.1073/pnas.160270897 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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