2EFF

Crystal structure analysis of the complex between CyaY and Co(II)

2EFF の概要

• エントリーDOI: 10.2210/pdb2eff/pdb
• 関連するPDBエントリー: 1EW4 1SOY
• 分子名称: Protein cyaY, COBALT (II) ION (3 entities in total)
• 機能のキーワード: frataxin, friedreich's ataxia iron binding, iron-sulfur cluster assembly, detoxifying redox-active iron, unknown function
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12360.22

構造登録者

Sica, F.,Franzese, M. (登録日: 2007-02-22, 公開日: 2007-10-02, 最終更新日: 2023-10-25)

主引用文献

Pastore, C.,Franzese, M.,Sica, F.,Temussi, P.,Pastore, A.
Understanding the binding properties of an unusual metal-binding protein - a study of bacterial frataxin
Febs J., 274:4199-4210, 2007

PubMed Abstract: Deficiency of the small mitochondrial protein frataxin causes Friedreich's ataxia, a severe neurodegenerative pathology. Frataxin, which has been highly conserved throughout evolution, is thought to be involved in, among other processes, Fe-S cluster formation. Independent evidence shows that it binds iron directly, although with very distinct features and low affinity. Here, we have carried out an extensive study of the binding properties of CyaY, the bacterial ortholog of frataxin, to different divalent and trivalent cations, using NMR and X-ray crystallography. We demonstrate that the protein has low cation specificity and contains multiple binding sites able to chelate divalent and trivalent metals with low affinity. Binding does not involve cavities or pockets, but exposed glutamates and aspartates, which are residues that are unusual for iron chelation when not assisted by histidines and/or cysteines. We have related how such an ability to bind cations on a relatively large area through an electrostatic mechanism could be a valuable asset for protein function.

PubMed: 17651435
DOI: 10.1111/j.1742-4658.2007.05946.x

実験手法

X-RAY DIFFRACTION (1.8 Å)