3CJK

Crystal structure of the adduct HAH1-Cd(II)-MNK1.

3CJK の概要

• エントリーDOI: 10.2210/pdb3cjk/pdb
• 関連するPDBエントリー: 1FE0 1KVI
• 分子名称: Copper transport protein ATOX1, Copper-transporting ATPase 1, CADMIUM ION, ... (4 entities in total)
• 機能のキーワード: hah1; atp7a; atp7b; menkes disease; metal homeostasis, chaperone, copper, copper transport, ion transport, metal-binding, transport, alternative splicing, atp-binding, cytoplasm, disease mutation, endoplasmic reticulum, glycoprotein, golgi apparatus, hydrolase, magnesium, membrane, nucleotide-binding, phosphoprotein, polymorphism, transmembrane, metal transport-hydrolase complex, metal transport/hydrolase
• 由来する生物種: Homo sapiens (Human); 詳細
• 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: 2
• 化学式量合計: 15824.46

構造登録者

Banci, L.,Bertini, I.,Calderone, V.,Felli, I.,Della-Malva, N.,Pavelkova, A.,Rosato, A. (登録日: 2008-03-13, 公開日: 2008-12-30, 最終更新日: 2023-08-30)

主引用文献

Banci, L.,Bertini, I.,Calderone, V.,Della-Malva, N.,Felli, I.C.,Neri, S.,Pavelkova, A.,Rosato, A.
Copper(I)-mediated protein-protein interactions result from suboptimal interaction surfaces.
Biochem.J., 422:37-42, 2009

PubMed Abstract: The homoeostasis of metal ions in cells is the result of the contribution of several cellular pathways that involve transient, often weak, protein-protein interactions. Metal transfer typically implies the formation of adducts where the metal itself acts as a bridge between proteins, by co-ordinating residues of both interacting partners. In the present study we address the interaction between the human copper(I)-chaperone HAH1 (human ATX1 homologue) and a metal-binding domain in one of its partners, namely the P-type copper-transporting ATPase, ATP7A (ATPase, Cu+ transporting, alpha polypeptide). The adduct was structurally characterized in solution, in the presence of copper(I), and through X-ray crystallography, upon replacing copper(I) with cadmium(II). Further insight was obtained through molecular modelling techniques and site-directed mutagenesis. It was found that the interaction involves a relatively small interface (less than 1000 A(2), 1 A=0.1 nm) with a low fraction of non-polar atoms. These observations provide a possible explanation for the low affinity of the two apoproteins. It appears that electrostatics is important in selecting which domain of the ATPase is able to form detectable amounts of the metal-mediated adduct with HAH1.

PubMed: 19453293
DOI: 10.1042/BJ20090422

実験手法

X-RAY DIFFRACTION (1.8 Å)