TY - JOUR
T1 - Reptile heme protein structure
T2 - X-ray crystallographic study of the aquo-met and cyano-met derivatives of the loggerhead sea turtle (Caretta caretta) myoglobin at 2.0 Å resolution
AU - Nardini, Marco
AU - Tarricone, Cataldo
AU - Rizzi, Menico
AU - Lania, Amalia
AU - Desideri, Alessandro
AU - De Sanctis, Gianpiero
AU - Coletta, Massimo
AU - Petruzzelli, Raffaele
AU - Ascenzi, Paolo
AU - Coda, Alessandro
AU - Bolognesi, Martino
PY - 1995
Y1 - 1995
N2 - 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 Å 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 Å. 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°.
AB - 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 Å 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 Å. 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°.
KW - Aquo-met myoglobin
KW - Cyano-met myoglobin
KW - Loggerhead sea turtle (Caretta caretta) myoglobin
KW - Monomeric heme protein
KW - X-ray protein structure
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M3 - Article
C2 - 7714901
AN - SCOPUS:0028955515
VL - 247
SP - 459
EP - 465
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 3
ER -