1b7z

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spinqualitylabelsall models 1b7z, resolution 2.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 FE and OXL 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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