Summary for 1B1X
| Entry DOI | 10.2210/pdb1b1x/pdb |
| Descriptor | LACTOFERRIN, FE (III) ION, CARBONATE ION, ... (4 entities in total) |
| Functional Keywords | iron binding protein, lactoferrin, antibacterial, metal binding protein |
| Biological source | Equus caballus (horse) |
| Cellular location | Secreted: O77811 |
| Total number of polymer chains | 1 |
| Total formula weight | 75602.91 |
| Authors | Sharma, A.K.,Srinivasan, A.,Singh, T.P. (deposition date: 1998-11-24, release date: 1999-06-24, Last modification date: 2024-04-03) |
| Primary citation | Sharma, A.K.,Paramasivam, M.,Srinivasan, A.,Yadav, M.P.,Singh, T.P. Three-dimensional structure of mare diferric lactoferrin at 2.6 A resolution. J.Mol.Biol., 289:303-317, 1999 Cited by PubMed Abstract: Lactoferrin is a monomeric glycoprotein with a molecular mass of approximately 80 kDa. The three-dimensional structure of mare diferric lactoferrin (mlf) has been determined at 2.6 A resolution. The protein crystallizes in the space group P 212121with a=85.2 A, b=99.5 A, c=103.1 A with a solvent content of 55 % (v/v). The structure was solved by the molecular replacement method using human diferric lactoferrin as the model. The structure has been refined using XPLOR to a final R -factor of 0.194 for all data in the 15-2.6 A resolution range. The amino acid sequence of mlf was determined using a cDNA method. The final refined model comprises 5281 protein atoms, 2 Fe3+, 2 CO32-and 112 water molecules. The overall folding of mlf is similar to that of other proteins of the transferrin family. The protein folds into two globular lobes, N and C. The lobes are further divided into two domains, N1 and N2, and C1 and C2. The iron-binding cleft is situated between the domains in each lobe. The N lobe appears to be well ordered and is more stable than the C lobe in mlf unlike in other lactoferrins, where the C lobe is the more stable. The opening of the binding cleft in the N lobe of mlf is narrower than those in other proteins of the transferrin family. This is very unusual and is found only in mare lactoferrin. Apart from certain hydrophobic interactions at the mouth of the cleft, one salt-bridge (Lys301 . . . . . . . . Glu216) crosses between the two walls of the cleft. The two lobes are connected covalently by a three-turn alpha-helix involving residues 334-344. The N lobe displays a highly ordered structure with appreciably low temperature factors. The iron coordination is more symmetrical in the N lobe than in the C lobe. There are only 16 intermolecular hydrogen bonds in the structure of mlf. PubMed: 10366507DOI: 10.1006/jmbi.1999.2767 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.62 Å) |
Structure validation
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