1FHA

SOLVING THE STRUCTURE OF HUMAN H FERRITIN BY GENETICALLY ENGINEERING INTERMOLECULAR CRYSTAL CONTACTS

1FHA の概要

• エントリーDOI: 10.2210/pdb1fha/pdb
• 分子名称: FERRITIN, FE (III) ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: iron storage, metal binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21390.61

構造登録者

Artymiuk, P.J.,Harrison, P.M. (登録日: 1990-12-20, 公開日: 1992-07-15, 最終更新日: 2024-02-07)

主引用文献

Lawson, D.M.,Artymiuk, P.J.,Yewdall, S.J.,Smith, J.M.,Livingstone, J.C.,Treffry, A.,Luzzago, A.,Levi, S.,Arosio, P.,Cesareni, G.,Thomas, C.D.,Shaw, W.V.,Harrison, P.M.
Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts.
Nature, 349:541-544, 1991

PubMed Abstract: Ferritin is important in iron homeostasis. Its twenty-four chains of two types, H and L, assemble as a hollow shell providing an iron-storage cavity. Ferritin molecules in cells containing high levels of iron tend to be rich in L chains, and may have a long-term storage function, whereas H-rich ferritins are more active in iron metabolism. The molecular basis for the greater activity of H-rich ferritins has until now been obscure, largely because the structure of H-chain ferritin has remained unknown owing to the difficulties in obtaining crystals ordered enough for X-ray crystallographic analysis. Here we report the three-dimensional structure of a human ferritin H-chain homopolymer. By genetically engineering a change in the sequence of the intermolecular contact region, we obtained crystals isomorphous with the homologous rat L ferritin and of high enough quality for X-ray diffraction analysis. The X-ray structure of human H ferritin shows a novel metal site embedded within each of its four-helix bundles and we suggest that ferroxidase activity associated with this site accounts for its rapid uptake of iron.

PubMed: 1992356
DOI: 10.1038/349541a0

実験手法

X-RAY DIFFRACTION (2.4 Å)