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 2.0&Aring;" /> '''LOGGERHEAD SEA TURTLE...)
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caption="1lhs, resolution 2.0&Aring;" />
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'''LOGGERHEAD SEA TURTLE MYOGLOBIN (AQUO-MET)'''<br />
'''LOGGERHEAD SEA TURTLE MYOGLOBIN (AQUO-MET)'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1LHS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caretta_caretta Caretta caretta] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LHS OCA].
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1LHS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Caretta_caretta Caretta caretta] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LHS OCA].
==Reference==
==Reference==
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[[Category: Nardini, M.]]
[[Category: Nardini, M.]]
[[Category: Petruzzelli, R.]]
[[Category: Petruzzelli, R.]]
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[[Category: Sanctis, G.De.]]
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[[Category: Sanctis, G De.]]
[[Category: Tarricone, C.]]
[[Category: Tarricone, C.]]
[[Category: HEM]]
[[Category: HEM]]
[[Category: oxygen storage]]
[[Category: oxygen storage]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:33:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:07 2008''

Revision as of 11:45, 21 February 2008


1lhs, resolution 2.0Å

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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 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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