1. Overproduction, purification, crystallization and preliminary X-ray analysis of the peroxiredoxin domain of a larger natural hybrid protein fromThermotoga maritima
- Author
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Nicolas Rouhier, Jean-Pierre Jacquot, Carole Barbey, Ahmed Haouz, Alda Navaza, Laboratoire de Biophysique Moléculaire Cellulaire et Tissulaire (BIOMOCETI), Université Paris 13 (UP13)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Interactions Arbres-Microorganismes (IAM), Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL), Cristallogenèse et Diffraction des Rayons X (Plate-forme/PF6), Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Université de Lorraine (UL)-Institut National de la Recherche Agronomique (INRA), Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris], Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), and Université Pierre et Marie Curie - Paris 6 (UPMC)-Université Paris 13 (UP13)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
0106 biological sciences ,MESH: Peroxiredoxins ,Crystallography, X-Ray ,medicine.disease_cause ,Polymerase Chain Reaction ,01 natural sciences ,Biochemistry ,law.invention ,MESH: Recombinant Proteins ,Nitroreductase ,MESH: Thermotoga maritima ,Structural Biology ,law ,Cloning, Molecular ,Overproduction ,MESH: Bacterial Proteins ,0303 health sciences ,biology ,MESH: Protein Multimerization ,Biological activity ,respiratory system ,Condensed Matter Physics ,Recombinant Proteins ,Crystallization Communications ,Recombinant DNA ,Two-hybrid screening ,Biophysics ,macromolecular substances ,peroxiredoxin domain ,03 medical and health sciences ,Bacterial Proteins ,Genetics ,medicine ,Thermotoga maritima ,MESH: Cloning, Molecular ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Escherichia coli ,030304 developmental biology ,MESH: Polymerase Chain Reaction ,Peroxiredoxins ,natural hybrid proteins ,equipment and supplies ,MESH: Crystallography, X-Ray ,biology.organism_classification ,biological sciences ,bacteria ,Protein Multimerization ,Peroxiredoxin ,010606 plant biology & botany - Abstract
International audience; Thermotoga maritima contains a natural hybrid protein constituted of two moieties: a peroxiredoxin domain at the N-terminus and a nitroreductase domain at the C-terminus. The peroxiredoxin (Prx) domain has been overproduced and purified from Escherichia coli cells. The recombinant Prx domain, which is homologous to bacterial Prx BCP and plant Prx Q, folds properly into a stable protein that possesses biological activity. The recombinant protein was crystallized and synchrotron data were collected to 2.9 Å resolution. The crystals belonged to the tetragonal space group I422, with unit-cell parameters a = b = 176.67, c = 141.20 Å.
- Published
- 2007
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