2ROP

Solution structure of domains 3 and 4 of human ATP7B

2ROP の概要

• エントリーDOI: 10.2210/pdb2rop/pdb
• NMR情報: BMRB: 11041
• 分子名称: Copper-transporting ATPase 2 (1 entity in total)
• 機能のキーワード: wilson protein, mobility, protein-protein interaction, alternative splicing, atp-binding, copper, copper transport, cytoplasm, disease mutation, golgi apparatus, hydrolase, ion transport, magnesium, membrane, metal-binding, mitochondrion, nucleotide-binding, phosphoprotein, polymorphism, transmembrane, transport
• 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: 21143.51

構造登録者

Banci, L.,Bertini, I.,Cantini, F.,Rosenzweig, A.C.,Yatsunyk, L.A. (登録日: 2008-04-04, 公開日: 2008-10-21, 最終更新日: 2024-05-15)

主引用文献

Banci, L.,Bertini, I.,Cantini, F.,Rosenzweig, A.C.,Yatsunyk, L.A.
Metal binding domains 3 and 4 of the Wilson disease protein: solution structure and interaction with the copper(I) chaperone HAH1
Biochemistry, 47:7423-7429, 2008

PubMed Abstract: The Wilson disease protein or ATP7B is a P 1B-type ATPase involved in human copper homeostasis. The extended N-terminus of ATP7B protrudes into the cytosol and contains six Cu(I) binding domains. This report presents the NMR structure of the polypeptide consisting of soluble Cu(I) binding domains 3 and 4. The two domains exhibit ferredoxin-like folds, are linked by a flexible loop, and act independently of one another. Domains 3 and 4 tend to aggregate in a concentration-dependent manner involving nonspecific intermolecular interactions. Both domains can be loaded with Cu(I) when provided as an acetonitrile complex or by the chaperone HAH1. HAH1 forms a 70% complex with domain 4 that is in fast exchange with the free protein in solution. The ability of HAH1 to form a complex only with some domains of ATP7B is an interesting property of this class of proteins and may have a signaling role in the function of the ATPases.

PubMed: 18558714
DOI: 10.1021/bi8004736

実験手法

SOLUTION NMR