2d3i | pdb_00002d3i
Crystal Structure of Aluminum-Bound Ovotransferrin at 2.15 Angstrom Resolution
Structural highlights
Function[TRFE_CHICK] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. Responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. There are two forms of hen transferrin, ovotransferrin, found in the ovoducts and, serum transferrin, secreted by the liver. Serum transferrin may also have a role in stimulating cell proliferation and is regulated by iron levels. Ovotransferrin has a bacteriostatic function and, is not controlled by iron levels. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTransferrin, well known as an iron-transport protein, can bind other metal ions, including toxic ones, and is considered to play an important role in the transportation of such metal ions. Here, a crystal structure of aluminium-bound transferrin is described for the first time. Colourless needle-shaped crystals of aluminium-bound ovotransferrin were obtained in PEG 400 solution. Structural determination was performed by molecular replacement using diferric (iron-bound) ovotransferrin as a model and the structural refinement was performed in the 50-2.15 Angstroms resolution range. The overall organization of the aluminium-bound form is almost the same as the iron-bound form: the protein is folded into two homologous lobes (N- and C-lobes) with two domains; two metal-binding sites are located within the inter-domain clefts of each lobe. Four residues (one Asp, two Tyr and one His) and one bicarbonate anion were found to bind an aluminium ion in either lobe, as in the iron-bound form. The highly similar domain-closed structure of the Al(3+)-bound form may permit the binding of Al(3+)-bound transferrin to the transferrin receptor. An unusual interaction, the dilysine trigger, which facilitates iron release at low pH in the endosome, was also found in the Al(3+)-bound form. These findings support the participation of transferrin in the transport of Al(3+) ions in vivo. Structure of aluminium-bound ovotransferrin at 2.15 Angstroms resolution.,Mizutani K, Mikami B, Aibara S, Hirose M Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1636-42. Epub 2005, Nov 19. PMID:16301797[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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