View source for 4bbj


==Copper-transporting PIB-ATPase in complex with beryllium fluoride representing the E2P state==
<StructureSection load='4bbj' size='340' side='right'caption='[[4bbj]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bbj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila Legionella pneumophila subsp. pneumophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BBJ 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]] 2.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene>, <scene name='pdbligand=CE1:O-DODECANYL+OCTAETHYLENE+GLYCOL'>CE1</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PC:PHOSPHOCHOLINE'>PC</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=4bbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bbj OCA], [https://pdbe.org/4bbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bbj RCSB], [https://www.ebi.ac.uk/pdbsum/4bbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bbj 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 metals in cells are typically regulated by PIB-type ATPases. The first structure of the class, a Cu+-ATPase from Legionella pneumophila (LpCopA), outlined a copper transport pathway across the membrane, which was inferred to be occluded. Here we show by molecular dynamics simulations that extracellular water solvated the transmembrane (TM) domain, results indicative of a Cu+-release pathway. Furthermore, a new LpCopA crystal structure determined at 2.8-A resolution, trapped in the preceding E2P state, delineated the same passage, and site-directed-mutagenesis activity assays support a functional role for the conduit. The structural similarities between the TM domains of the two conformations suggest that Cu+-ATPases couple dephosphorylation and ion extrusion differently than do the well-characterized PII-type ATPases. The ion pathway explains why certain Menkes' and Wilson's disease mutations impair protein function and points to a site for inhibitors targeting pathogens.

Copper-transporting P-type ATPases use a unique ion-release pathway.,Andersson M, Mattle D, Sitsel O, Klymchuk T, Nielsen AM, Moller LB, White SH, Nissen P, Gourdon P Nat Struct Mol Biol. 2013 Dec 8. doi: 10.1038/nsmb.2721. PMID:24317491<ref>PMID:24317491</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bbj" 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]]
[[Category: Gourdon P]]
[[Category: Mattle D]]
[[Category: Nissen P]]