View source for 3rfu


==Crystal structure of a copper-transporting PIB-type ATPase==
<StructureSection load='3rfu' size='340' side='right'caption='[[3rfu]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3rfu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._Philadelphia_1 Legionella pneumophila subsp. pneumophila str. Philadelphia 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RFU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RFU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rfu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rfu OCA], [https://pdbe.org/3rfu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rfu RCSB], [https://www.ebi.ac.uk/pdbsum/3rfu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rfu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COPA_LEGPH COPA_LEGPH] Couples the hydrolysis of ATP with the export of copper.<ref>PMID:24317491</ref> <ref>PMID:34826402</ref> <ref>PMID:21716286</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 A 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.

Crystal structure of a copper-transporting PIB-type ATPase.,Gourdon P, Liu XY, Skjorringe T, Morth JP, Moller LB, Pedersen BP, Nissen P Nature. 2011 Jun 29;475(7354):59-64. doi: 10.1038/nature10191. PMID:21716286<ref>PMID:21716286</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3rfu" style="background-color:#fffaf0;"></div>

==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]]
[[Category: Birk Moller L]]
[[Category: Gourdon P]]
[[Category: Liu X]]
[[Category: Morth JP]]
[[Category: Nissen P]]
[[Category: Panyella Pedersen B]]
[[Category: Skjorringe T]]