1lhs
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(New page: 200px<br /><applet load="1lhs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lhs, resolution 2.0Å" /> '''LOGGERHEAD SEA TURTLE...)
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Revision as of 18:26, 20 November 2007
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LOGGERHEAD SEA TURTLE MYOGLOBIN (AQUO-MET)
Overview
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.
About this Structure
1LHS is a Single protein structure of sequence from Caretta caretta with HEM as ligand. Full crystallographic information is available from OCA.
Reference
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., Nardini M, Tarricone C, Rizzi M, Lania A, Desideri A, De Sanctis G, Coletta M, Petruzzelli R, Ascenzi P, Coda A, et al., J Mol Biol. 1995 Mar 31;247(3):459-65. PMID:7714901
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