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  • Title: Structural studies on the loggerhead sea turtle (Caretta caretta) myoglobin.
    Author: Petruzzelli R, Aureli G, Casale E, Nardini M, Rizzi M, Ascenzi P, Coletta M, De Sanctis G, Desideri A, Galtieri A.
    Journal: Biochem Mol Biol Int; 1993 Sep; 31(1):19-24. PubMed ID: 8260943.
    Abstract:
    The primary structure of myoglobin from the loggerhead sea turtle (Caretta caretta) has been determined; the protein consists of 153 amino acid residues. The ferric loggerhead sea turtle myoglobin has been crystallized in a form suitable for X-ray structural investigations. The crystals were grown at pH 8.0, in 0.05 M tris/HCl buffer, using 3.2 M ammonium sulfate as precipitating agent, at 4 degrees C, and belong to the orthorhombic space group P2(1)2(1)2(1), with unit cell constants a = 37.2 A, b = 61.1 A, c = 75.2 A (one molecule, 17,000 M(r), in the asymmetric unit). A molecular replacement solution was found for the loggerhead sea turtle myoglobin crystals using sperm whale myoglobin structure as search model. The R-factor value, after molecular replacement, is 0.387, for the data in the 15-3.3 A resolution range. The results here reported are the basis for the first X-ray crystallographic investigation on a reptile myoglobin, and indicate a strong overall structural similarity between the loggerhead sea turtle and mammalian (i.e. sperm whale) myoglobins.
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