1FCK

STRUCTURE OF DICERIC HUMAN LACTOFERRIN

1FCK の概要

• エントリーDOI: 10.2210/pdb1fck/pdb
• 関連するPDBエントリー: 1cb6 1lct 1lfg 1lfi
• 分子名称: LACTOFERRIN, CARBONATE ION, CERIUM (III) ION, ... (4 entities in total)
• 機能のキーワード: transferrin, metal-binding, cerium, lanthanide, metal transport
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P02788
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 76806.69

構造登録者

Baker, H.M.,Baker, C.J.,Smith, C.A.,Baker, E.N. (登録日: 2000-07-18, 公開日: 2001-01-17, 最終更新日: 2024-11-06)

主引用文献

Baker, H.M.,Baker, C.J.,Smith, C.A.,Baker, E.N.
Metal substitution in transferrins: specific binding of cerium(IV) revealed by the crystal structure of cerium-substituted human lactoferrin.
J.Biol.Inorg.Chem., 5:692-698, 2000

PubMed Abstract: Proteins of the transferrin family play a key role in iron homeostasis through their extremely strong binding of iron, as Fe3+. They are nevertheless able to bind a surprisingly wide variety of other metal ions. To investigate how metal ions of different size, charge and coordination characteristics are accommodated, we have determined the crystal structure of human lactoferrin (Lf) complexed with Ce4+. The structure, refined at 2.2 A resolution (R=20.2%, Rfree=25.7%) shows that the two Ce4+ ions occupy essentially the same positions as do Fe3+, and that the overall protein structure is unchanged; the same closed structure is formed for Ce2Lf as for Fe2Lf. The larger metal ion is accommodated by small shifts in the protein ligands, made possible by the presence of water molecules adjacent to each binding site. The two Ce4+ sites are equally occupied, indicating that the known difference in the pH-dependent release of Ce4+ arises from a specific protonation event, possibly of the His ligand in one of the binding sites. Comparing the effects of binding Ce4+ with those for the binding of other metal ions, we conclude that the ability of transferrins to accommodate metal ions other than Fe3+ depends on an interplay of charge, size, coordination and geometrical preferences of the bound metal ion. However, it is the ability to accept the six-coordinate, approximately octahedral, site provided by the protein that is of greatest importance.

PubMed: 11128996
DOI: 10.1007/s007750000157

実験手法

X-RAY DIFFRACTION (2.2 Å)