1B7Z

STRUCTURE OF OXALATE SUBSTITUTED DIFERRIC MARE LACTOFERRIN FROM COLOSTRUM

Summary for 1B7Z

• Entry DOI: 10.2210/pdb1b7z/pdb
• Descriptor: PROTEIN (LACTOFERRIN), FE (III) ION, OXALATE ION, ... (4 entities in total)
• Functional Keywords: lactoferrin, dioxalate, metal binding site, metal transport
• Biological source: Equus caballus (horse)
• Total number of polymer chains: 1
• Total formula weight: 75658.93

Authors

Sharma, A.K.,Singh, T.P. (deposition date: 1999-01-26, release date: 1999-02-02, Last modification date: 2024-11-06)

Primary citation

Sharma, A.K.,Singh, T.P.
Structure of oxalate-substituted diferric mare lactoferrin at 2.7 A resolution.
Acta Crystallogr.,Sect.D, 55:1792-1798, 1999

PubMed Abstract: 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.

PubMed: 10531474
DOI: 10.1107/S0907444999009439

Experimental method

X-RAY DIFFRACTION (2.7 Å)