Crystal structure of Escherichia coli CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family
| Autor: | Jin Kuk Yang, Se Won Suh, Jae Young Lee, Hyun Kyu Song, Myong Gyong Lee, Seung Je Cho |
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| Rok vydání: | 2000 |
| Předmět: |
Protein Folding
Databases Factual Protein family Protein Conformation Molecular Sequence Data Mutation Missense Crystallography X-Ray medicine.disease_cause Evolution Molecular Protein structure Bacterial Proteins Iron-Binding Proteins medicine Amino Acid Sequence Escherichia coli Peptide sequence Gene Genetics Multidisciplinary Sequence Homology Amino Acid biology Escherichia coli Proteins Iron-binding proteins Biological Sciences Phosphotransferases (Alcohol Group Acceptor) Frataxin biology.protein Protein folding |
| Zdroj: | Proceedings of the National Academy of Sciences. 97:8932-8937 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.160270897 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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