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Lactoferrin binds two Fe3+ 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 Å resolution. The final model has a crystallographic R factor of 21.3% for all data in the resolution range 17.0-2.7 Å. 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.

Supporting information

PDB reference: oxalate-substituted diferric mare lactoferrin, 1b7z

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