Crystallization and preliminary X-ray crystallographic analysis ofEscherichia coliCyaY, a structural homologue of human frataxin
| Autor: | Jin Kuk Yang, Seung Je Cho, Hyun Kyu Song, Se Won Suh, Myong Gyong Lee |
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| Rok vydání: | 2000 |
| Předmět: |
Protein Conformation
Saccharomyces cerevisiae Polyethylene glycol Mitochondrion Crystallography X-Ray medicine.disease_cause law.invention chemistry.chemical_compound Bacterial Proteins Structural Biology law Iron-Binding Proteins Escherichia coli medicine Humans Molecule Crystallization biology Escherichia coli Proteins General Medicine biology.organism_classification Recombinant Proteins Phosphotransferases (Alcohol Group Acceptor) Crystallography chemistry Biochemistry Frataxin biology.protein Recombinant DNA |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 56:920-921 |
| ISSN: | 0907-4449 |
| DOI: | 10.1107/s0907444900005916 |
| Popis: | CyaY is a 106-residue protein from Escherichia coli. It shows amino-acid sequence similarity to human frataxin and a frataxin homologue in Saccharomyces cerevisiae, Yfh1p. The former is associated with the disease Friedreich ataxia and the latter plays a key role in iron homeostasis in mitochondria. CyaY has been overexpressed in soluble form in E. coli. The recombinant protein with a His(6) tag at its C-terminus has been crystallized at 296 K using polyethylene glycol (PEG) 4000 as a precipitant. Native diffraction data have been collected to 1.8 A using Cu Kalpha X-rays. The crystals belong to the trigonal space group P3(1)21 (or P3(2)21), with unit-cell parameters a = b = 44.66, c = 99.87 A, alpha = beta = 90.0, gamma = 120.0 degrees. The asymmetric unit contains one molecule of recombinant CyaY, with a corresponding V(m) of 2.13 A(3) Da(-1) and solvent content of 42.3%. |
| Databáze: | OpenAIRE |
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