Structural studies on the loggerhead sea turtle (Caretta caretta) myoglobin.
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.
Petruzzelli
R
R
Dipartimento di Biologia, Università di Roma, Tor Vergata, Italy.
Aureli
G
G
Casale
E
E
Nardini
M
M
Rizzi
M
M
Ascenzi
P
P
Coletta
M
M
De Sanctis
G
G
Desideri
A
A
Galtieri
A
A
D000595:Amino Acid Sequence; D000818:Animals; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D009211:Myoglobin / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D011487:Protein Conformation; D016415:Sequence Alignment; D014426:Turtles
D009211:Myoglobin