2CN7
Recombinant human H ferritin, K86Q, E27D and E107D mutant
2CN7 の概要
エントリーDOI | 10.2210/pdb2cn7/pdb |
関連するPDBエントリー | 1FHA 2CEI 2CHI 2CIH 2CLU 2CN6 2FHA |
分子名称 | FERRITIN HEAVY CHAIN, CALCIUM ION, GLYCEROL, ... (4 entities in total) |
機能のキーワード | oxidoreductase, iron, apoferritin, ferroxidase, iron storage, metal-binding, phosphorylation, di-iron non-heme 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 | 21438.88 |
構造登録者 | |
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 Cited by 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: 17070541DOI: 10.1016/J.JMB.2006.10.010 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.75 Å) |
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