3RFU

Crystal structure of a copper-transporting PIB-type ATPase

Summary for 3RFU

• Entry DOI: 10.2210/pdb3rfu/pdb
• Descriptor: Copper efflux ATPase, TETRAFLUOROALUMINATE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: 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
• Biological source: Legionella pneumophila subsp. pneumophila
• Total number of polymer chains: 4
• Total formula weight: 313989.10

Authors

Gourdon, P.,Liu, X.,Skjorringe, T.,Morth, J.P.,Birk Moller, L.,Panyella Pedersen, B.,Nissen, P. (deposition date: 2011-04-07, release date: 2011-06-29, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.2 Å)