7pge

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<StructureSection load='7pge' size='340' side='right'caption='[[7pge]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='7pge' size='340' side='right'caption='[[7pge]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7pge]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PGE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7pge]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PGE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</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=7pge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pge OCA], [https://pdbe.org/7pge PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pge RCSB], [https://www.ebi.ac.uk/pdbsum/7pge PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pge ProSAT]</span></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=7pge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pge OCA], [https://pdbe.org/7pge PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pge RCSB], [https://www.ebi.ac.uk/pdbsum/7pge PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pge ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PCOB_ECOLX PCOB_ECOLX]] Required for the copper-inducible expression of copper resistance.
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[[https://www.uniprot.org/uniprot/PCOB_ECOLX PCOB_ECOLX]] Required for the copper-inducible expression of copper resistance.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Copper (Cu) is one of the most abundant trace metals in all organisms, involved in a plethora of cellular processes. Yet elevated concentrations of the element are harmful, and interestingly prokaryotes are more sensitive for environmental Cu stress than humans. Various transport systems are present to maintain intracellular Cu homeostasis, including the prokaryotic plasmid-encoded multiprotein pco operon, which is generally assigned as a defense mechanism against elevated Cu concentrations. Here we structurally and functionally characterize the outer membrane component of the Pco system, PcoB, recovering a 2.0 A structure, revealing a classical beta-barrel architecture. Unexpectedly, we identify a large opening on the extracellular side, linked to a considerably electronegative funnel that becomes narrower towards the periplasm, defining an ion-conducting pathway as also supported by metal binding quantification via inductively coupled plasma mass spectrometry and molecular dynamics (MD) simulations. However, the structure is partially obstructed towards the periplasmic side, and yet flux is permitted in the presence of a Cu gradient as shown by functional characterization in vitro. Complementary in vivo experiments demonstrate that isolated PcoB confers increased sensitivity towards Cu. Aggregated, our findings indicate that PcoB serves to permit Cu import. Thus, it is possible the Pco system physiologically accumulates Cu in the periplasm as a part of an unorthodox defense mechanism against metal stress. These results point to a previously unrecognized principle of maintaining Cu homeostasis and may as such also assist in the understanding and in efforts towards combatting bacterial infections of Pco-harboring pathogens.
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PcoB is a defense outer membrane protein that facilitates cellular uptake of copper.,Li P, Nayeri N, Gorecki K, Becares ER, Wang K, Mahato DR, Andersson M, Abeyrathna SS, Lindkvist-Petersson K, Meloni G, Missel JW, Gourdon P Protein Sci. 2022 Jul;31(7):e4364. doi: 10.1002/pro.4364. PMID:35762724<ref>PMID:35762724</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7pge" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gourdon, P E]]
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[[Category: Gourdon PE]]
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[[Category: Li, P]]
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[[Category: Li P]]
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[[Category: Transport protein]]
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[[Category: Transporter]]
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Revision as of 06:24, 8 September 2022

copper transporter PcoB

PDB ID 7pge

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