3RFU

Crystal structure of a copper-transporting PIB-type ATPase

3RFU の概要

• エントリーDOI: 10.2210/pdb3rfu/pdb
• 分子名称: Copper efflux ATPase, TETRAFLUOROALUMINATE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: alpha helical, cpc, cxxc, atp-binding, hydrolase, ion transport, magnesium, cu+, membrane, metal-binding, nucleotide-binding, potassium, transmembrane, transport, heavy-metal binding, p-type atpase, pib-atpase, cu+ exporting, copper transport, pi-atpase, membrane protein
• 由来する生物種: Legionella pneumophila subsp. pneumophila
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 313989.10

構造登録者

Gourdon, P.,Liu, X.,Skjorringe, T.,Morth, J.P.,Birk Moller, L.,Panyella Pedersen, B.,Nissen, P. (登録日: 2011-04-07, 公開日: 2011-06-29, 最終更新日: 2024-02-21)

主引用文献

Gourdon, P.,Liu, X.Y.,Skjorringe, T.,Morth, J.P.,Moller, L.B.,Pedersen, B.P.,Nissen, P.
Crystal structure of a copper-transporting PIB-type ATPase.
Nature, 475:59-64, 2011

PubMed Abstract: Heavy-metal homeostasis and detoxification is crucial for cell viability. P-type ATPases of the class IB (PIB) are essential in these processes, actively extruding heavy metals from the cytoplasm of cells. Here we present the structure of a PIB-ATPase, a Legionella pneumophila CopA Cu(+)-ATPase, in a copper-free form, as determined by X-ray crystallography at 3.2 Å resolution. The structure indicates a three-stage copper transport pathway involving several conserved residues. A PIB-specific transmembrane helix kinks at a double-glycine motif displaying an amphipathic helix that lines a putative copper entry point at the intracellular interface. Comparisons to Ca(2+)-ATPase suggest an ATPase-coupled copper release mechanism from the binding sites in the membrane via an extracellular exit site. The structure also provides a framework to analyse missense mutations in the human ATP7A and ATP7B proteins associated with Menkes' and Wilson's diseases.

PubMed: 21716286
DOI: 10.1038/nature10191

実験手法

X-RAY DIFFRACTION (3.2 Å)