View source for 4f2f


==Crystal structure of the metal binding domain (MBD) of the Streptococcus pneumoniae D39 Cu(I) exporting P-type ATPase CopA with Cu(I)==
<StructureSection load='4f2f' size='340' side='right'caption='[[4f2f]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4f2f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_D39 Streptococcus pneumoniae D39]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F2F FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</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=4f2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f2f OCA], [https://pdbe.org/4f2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f2f RCSB], [https://www.ebi.ac.uk/pdbsum/4f2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f2f ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0H2ZQ91_STRP2 A0A0H2ZQ91_STRP2] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Copper resistance has emerged as an important virulence determinant of microbial pathogens. In Streptococcus pneumoniae, copper resistance is mediated by the copper-responsive repressor CopY, CupA and the copper-effluxing P(1B)-type ATPase CopA. We show here that CupA is a previously uncharacterized cell membrane-anchored Cu(I) chaperone and that a Cu(I) binding-competent, membrane-localized CupA is obligatory for copper resistance. The crystal structures of the soluble domain of CupA and the N-terminal metal-binding domain (MBD) of CopA (CopA(MBD)) reveal isostructural cupredoxin-like folds that each harbor a binuclear Cu(I) cluster unprecedented in bacterial copper trafficking. NMR studies reveal unidirectional Cu(I) transfer from the low-affinity site on the soluble domain of CupA to the high-affinity site of CopA(MBD). However, copper binding by CopA(MBD) is not essential for cellular copper resistance, consistent with a primary role of CupA in cytoplasmic Cu(I) sequestration and/or direct delivery to the transmembrane site of CopA for cellular efflux.

A new structural paradigm in copper resistance in Streptococcus pneumoniae.,Fu Y, Tsui HC, Bruce KE, Sham LT, Higgins KA, Lisher JP, Kazmierczak KM, Maroney MJ, Dann CE 3rd, Winkler ME, Giedroc DP Nat Chem Biol. 2013 Jan 27. doi: 10.1038/nchembio.1168. PMID:23354287<ref>PMID:23354287</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4f2f" style="background-color:#fffaf0;"></div>

==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae D39]]
[[Category: Dann III CE]]
[[Category: Fu Y]]
[[Category: Giedroc DP]]