Reptile heme protein structure: X-ray crystallographic study of the aquo-met and cyano-met derivatives of the loggerhead sea turtle (Caretta caretta) myoglobin at 2.0 A resolution

• Published in: Journal of molecular biology 1995-03, Vol.247 (3), p.459-465
• Main Authors: Nardini, M, Tarricone, C, Rizzi, M, Lania, A, Desideri, A, De Sanctis, G, Coletta, M, Petruzzelli, R, Ascenzi, P, Coda, A
• Format: Article
• Language: English
• Subjects: Animals; Azides - metabolism; Binding Sites; Crystallography, X-Ray; Cyanides - metabolism; Heme - chemistry; Mammals - metabolism; Metmyoglobin - analogs & derivatives; Metmyoglobin - chemistry; Models, Molecular; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Reptiles - metabolism; Sequence Homology, Amino Acid; Species Specificity; Turtles - metabolism; Water - chemistry
• ISSN: 0022-2836
• DOI: 10.1006/jmbi.1994.0153

The X-ray crystal structures of the aquo-met and cyano-met derivatives of the loggerhead sea turtle (Caretta caretta) myoglobin have been determined at 2.0 A resolution (R = 0.182, and 0.178, respectively). The results here reported, representing the first reptile globin solved by X-ray crystallography, have been analyzed in parallel with data for related monomeric hemoproteins, and indicate a strong overall structural similarity between the loggerhead sea turtle and mammalian myoglobins, reflected by the 63% amino acid identity of their primary structures. The root-mean-square deviation between the entire polypeptide backbones of loggerhead sea turtle and sperm whale myoglobins, after structure superposition, is 0.83 A. Upon cyanide binding to the protein distal site, the iron-bound water molecule present in the aquo-met form is displaced by the incoming ligand. Cyanide is oriented towards the inner part of the heme distal site forming a Fe-C-N angle of 133 degrees.