2CEI

Recombinant human H ferritin, K86Q mutant, soaked with Zn

2CEI の概要

• エントリーDOI: 10.2210/pdb2cei/pdb
• 関連するPDBエントリー: 1FHA 2FHA
• 分子名称: FERRITIN HEAVY CHAIN, ZINC ION (3 entities in total)
• 機能のキーワード: apoferritin, ferroxidase, di-iron, non-heme protein, iron storage, oxidoreductase
• 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: 21777.88

構造登録者

Toussaint, L.,Crichton, R.R.,Declercq, J.P. (登録日: 2006-02-07, 公開日: 2006-12-13, 最終更新日: 2023-12-13)

主引用文献

Toussaint, L.,Bertrand, L.,Hue, L.,Crichton, R.R.,Declercq, J.P.
High-Resolution X-Ray Structures of Human Apoferritin H-Chain Mutants Correlated with Their Activity and Metal-Binding Sites.
J.Mol.Biol., 365:440-, 2007

PubMed Abstract: Ferritins are a family of proteins distributed widely in nature. In bacterial, plant, and animal cells, ferritin appears to serve as a soluble, bioavailable, and non-toxic form of iron provider. Ferritins from animal sources are heteropolymers composed of two types of subunit, H and L, which differ mainly by the presence (H) or absence (L) of active ferroxidase centres. We report the crystallographic structures of four human H apoferritin variants at a resolution of up to 1.5 Angstrom. Crystal derivatives using Zn(II) as redox-stable alternative for Fe(II), allows us to characterize the different metal-binding sites. The ferroxidase centre, which is composed of sites A and B, binds metal with a preference for the A site. In addition, distinct Zn(II)-binding sites were found in the 3-fold axes, 4-fold axes and on the cavity surface near the ferroxidase centre. To study the importance of the distance of the two metal atoms in the ferroxidase centre, single and double replacement of glutamate 27 (site A) and glutamate 107 (site B), the two axial ligands, by aspartate residues have been carried out. The consequences for metal binding and the correlation with Fe(II) oxidation rates are discussed.

PubMed: 17070541
DOI: 10.1016/J.JMB.2006.10.010

実験手法

X-RAY DIFFRACTION (1.8 Å)