6z9n
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Copper transporter OprC== | |
| + | <StructureSection load='6z9n' size='340' side='right'caption='[[6z9n]], [[Resolution|resolution]] 2.73Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6z9n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Z9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Z9N 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]] 2.73Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=6z9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6z9n OCA], [https://pdbe.org/6z9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6z9n RCSB], [https://www.ebi.ac.uk/pdbsum/6z9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6z9n ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/G3XD89_PSEAE G3XD89_PSEAE] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Copper, while toxic in excess, is an essential micronutrient in all kingdoms of life due to its essential role in the structure and function of many proteins. Proteins mediating ionic copper import have been characterised in detail for eukaryotes, but much less so for prokaryotes. In particular, it is still unclear whether and how gram-negative bacteria acquire ionic copper. Here, we show that Pseudomonas aeruginosa OprC is an outer membrane, TonB-dependent transporter that is conserved in many Proteobacteria and which mediates acquisition of both reduced and oxidised ionic copper via an unprecedented CxxxM-HxM metal binding site. Crystal structures of wild-type and mutant OprC variants with silver and copper suggest that acquisition of Cu(I) occurs via a surface-exposed "methionine track" leading towards the principal metal binding site. Together with whole-cell copper quantitation and quantitative proteomics in a murine lung infection model, our data identify OprC as an abundant component of bacterial copper biology that may enable copper acquisition under a wide range of conditions. | ||
| - | + | Acquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.,Bhamidimarri SP, Young TR, Shanmugam M, Soderholm S, Basle A, Bumann D, van den Berg B PLoS Biol. 2021 Nov 11;19(11):e3001446. doi: 10.1371/journal.pbio.3001446., eCollection 2021 Nov. PMID:34762655<ref>PMID:34762655</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6z9n" style="background-color:#fffaf0;"></div> |
| - | [[Category: Bhamidimarri | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas aeruginosa PAO1]] | ||
| + | [[Category: Bhamidimarri SP]] | ||
| + | [[Category: Van den Berg B]] | ||
Current revision
Copper transporter OprC
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