1Y3J

Solution structure of the copper(I) form of the fifth domain of Menkes protein

1Y3J の概要

• エントリーDOI: 10.2210/pdb1y3j/pdb
• 関連するPDBエントリー: 1Y3K
• 分子名称: Copper-transporting ATPase 1, COPPER (II) ION (2 entities in total)
• 機能のキーワード: ferrodoxin-like fold, beta-alpha-beta-beta-alpha-beta structure, structural proteomics in europe, spine, structural genomics, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Isoform 3: Cytoplasm, cytosol (Probable). Isoform 5: Endoplasmic reticulum: Q04656
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8549.39

構造登録者

Banci, L.,Chasapis, C.T.,Ciofi-Baffoni, S.,Hadjiliadis, N.,Rosato, A.,Structural Proteomics in Europe (SPINE) (登録日: 2004-11-25, 公開日: 2005-03-08, 最終更新日: 2024-05-29)

主引用文献

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Chasapis, C.T.,Hadjiliadis, N.,Rosato, A.
An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes protein
Febs J., 272:865-871, 2005

PubMed Abstract: The interaction between the human copper(I) chaperone, HAH1, and one of its two physiological partners, the Menkes disease protein (ATP7A), was investigated in solution using heteronuclear NMR. The study was carried out through titrations involving HAH1 and either the second or the fifth soluble domains of ATP7A (MNK2 and MNK5, respectively), in the presence of copper(I). The copper-transfer properties of MNK2 and MNK5 are similar, and differ significantly from those previously observed for the yeast homologous system. In particular, no stable adduct is formed between either of the MNK domains and HAH1. The copper(I) transfer reaction is slow on the time scale of the NMR chemical shift, and the equilibrium is significantly shifted towards the formation of copper(I)-MNK2/MNK5. The solution structures of both apo- and copper(I)-MNK5, which were not available, are also reported. The results are discussed in comparison with the data available in the literature for the interaction between HAH1 and its partners from other spectroscopic techniques.

PubMed: 15670166
DOI: 10.1111/j.1742-4658.2004.04526.x

実験手法

SOLUTION NMR