1b7z

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(New page: 200px<br /><applet load="1b7z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b7z, resolution 2.7&Aring;" /> '''STRUCTURE OF OXALATE ...)
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'''STRUCTURE OF OXALATE SUBSTITUTED DIFERRIC MARE LACTOFERRIN FROM COLOSTRUM'''<br />
'''STRUCTURE OF OXALATE SUBSTITUTED DIFERRIC MARE LACTOFERRIN FROM COLOSTRUM'''<br />
==Overview==
==Overview==
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Lactoferrin binds two Fe(3+) and two CO(2-)(3) ions with high affinity. It, can also bind other metal ions and anions. In order to determine the, perturbations in the environments of the binding sites in the N and C, lobes and elsewhere in the protein, the crystal structure of, oxalate-substituted diferric mare lactoferrin has been determined at 2.7 A, resolution. The final model has a crystallographic R factor of 21.3% for, all data in the resolution range 17.0-2.7 A. The substitution of an, oxalate anion does not perturb the overall structure of the protein, but, produces several significant changes at the metal-binding and, anion-binding sites. The binding of the oxalate anion is symmetrical in, both the N and C lobes, unlike in diferric dioxalate human lactoferrin, where the oxalate anion binds the metal ion symmetrically in the C lobe, and asymmetrically in the N lobe.
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Lactoferrin binds two Fe(3+) and two CO(2-)(3) ions with high affinity. It can also bind other metal ions and anions. In order to determine the perturbations in the environments of the binding sites in the N and C lobes and elsewhere in the protein, the crystal structure of oxalate-substituted diferric mare lactoferrin has been determined at 2.7 A resolution. The final model has a crystallographic R factor of 21.3% for all data in the resolution range 17.0-2.7 A. The substitution of an oxalate anion does not perturb the overall structure of the protein, but produces several significant changes at the metal-binding and anion-binding sites. The binding of the oxalate anion is symmetrical in both the N and C lobes, unlike in diferric dioxalate human lactoferrin, where the oxalate anion binds the metal ion symmetrically in the C lobe and asymmetrically in the N lobe.
==About this Structure==
==About this Structure==
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1B7Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with FE and OXL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B7Z OCA].
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1B7Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=OXL:'>OXL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B7Z OCA].
==Reference==
==Reference==
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[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Sharma, A.K.]]
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[[Category: Sharma, A K.]]
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[[Category: Singh, T.P.]]
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[[Category: Singh, T P.]]
[[Category: FE]]
[[Category: FE]]
[[Category: OXL]]
[[Category: OXL]]
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[[Category: metal binding site]]
[[Category: metal binding site]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:26:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:31 2008''

Revision as of 09:52, 21 February 2008

Image:1b7z.jpg

1b7z, resolution 2.7Å

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STRUCTURE OF OXALATE SUBSTITUTED DIFERRIC MARE LACTOFERRIN FROM COLOSTRUM

Overview

Lactoferrin binds two Fe(3+) and two CO(2-)(3) ions with high affinity. It can also bind other metal ions and anions. In order to determine the perturbations in the environments of the binding sites in the N and C lobes and elsewhere in the protein, the crystal structure of oxalate-substituted diferric mare lactoferrin has been determined at 2.7 A resolution. The final model has a crystallographic R factor of 21.3% for all data in the resolution range 17.0-2.7 A. The substitution of an oxalate anion does not perturb the overall structure of the protein, but produces several significant changes at the metal-binding and anion-binding sites. The binding of the oxalate anion is symmetrical in both the N and C lobes, unlike in diferric dioxalate human lactoferrin, where the oxalate anion binds the metal ion symmetrically in the C lobe and asymmetrically in the N lobe.

About this Structure

1B7Z is a Single protein structure of sequence from Equus caballus with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of oxalate-substituted diferric mare lactoferrin at 2.7 A resolution., Sharma AK, Singh TP, Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1792-8. PMID:10531474

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