1QJM
Crystal Structure of a Complex of Lactoferrin with a Lanthanide Ion (SM3+) at 3.4 Angstrom Resolution
Summary for 1QJM
Entry DOI | 10.2210/pdb1qjm/pdb |
Descriptor | LACTOFERRIN, SAMARIUM (III) ION, CARBONATE ION (3 entities in total) |
Functional Keywords | lactoferrin, complex, iron binding, transferrin |
Biological source | EQUUS CABALLUS (HORSE) |
Total number of polymer chains | 1 |
Total formula weight | 75791.94 |
Authors | Sharma, A.K.,Singh, T.P. (deposition date: 1999-06-27, release date: 1999-08-26, Last modification date: 2024-11-13) |
Primary citation | Sharma, A.K.,Singh, T.P. Lactoferrin-Metal Interactions: First Crystal Structure of a Complex of Lactoferrin with a Lanthanide Ion (Sm3+) at 3.4 Angstrom Resolution Acta Crystallogr.,Sect.D, 55:1799-, 1999 Cited by PubMed Abstract: Lactoferrin is an important member of the transferrin family. A characteristic property of transferrins is their ability to bind very tightly (K(app) approximately/= 10(20)) but reversibly two Fe(3+) ions. The structural consequences of binding a metal other than Fe(3+) have been examined by crystallographic analysis at 3.4 A resolution of mare samarium-lactoferrin (Sm(2)Lf). The structure was refined to an R factor of 0.219 for 8776 reflections in the resolution range 17.0-3.4 A. The samarium geometry (distorted octahedral coordination) is similar in both lobes. However, the anion interactions are quite different in the two lobes. In the N lobe, the anion is able to form only two hydrogen bonds instead of the four observed in the C lobe of Sm(2)Lf and the six observed in Fe(2)Lf. This is because Arg121, Thr117 and Gly124 have moved away from the anion as a consequence of the binding of the Sm(3+) ion. The protein ligands in the binding cleft of Sm(2)Lf show large displacements, but the overall protein structure remains the same. The binding of Sm(3+) by lactoferrin shows that the protein is capable of sequestering ions of different sizes and charges, though with reduced affinity. This conclusion should be true of other transferrins also. PubMed: 10531475DOI: 10.1107/S0907444999009865 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
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