3pik

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<StructureSection load='3pik' size='340' side='right'caption='[[3pik]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3pik' size='340' side='right'caption='[[3pik]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3pik]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PIK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PIK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3pik]] 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=3PIK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PIK FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cusC, ibeB, ylcB, b0572, JW0561 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNL:UNKNOWN+LIGAND'>UNL</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=3pik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pik OCA], [https://pdbe.org/3pik PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pik RCSB], [https://www.ebi.ac.uk/pdbsum/3pik PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pik 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=3pik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pik OCA], [https://pdbe.org/3pik PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pik RCSB], [https://www.ebi.ac.uk/pdbsum/3pik PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pik ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CUSC_ECOLI CUSC_ECOLI]] Part of a cation efflux system that mediates resistance to copper and silver. In pathogenic strains it allows the bacteria to invade brain microvascular endothelial cells (BMEC) thus allowing it to cross the blood-brain barrier and cause neonatal meningitis.<ref>PMID:11399769</ref> <ref>PMID:12813074</ref>
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[https://www.uniprot.org/uniprot/CUSC_ECOLI CUSC_ECOLI] Part of a cation efflux system that mediates resistance to copper and silver. In pathogenic strains it allows the bacteria to invade brain microvascular endothelial cells (BMEC) thus allowing it to cross the blood-brain barrier and cause neonatal meningitis.<ref>PMID:11399769</ref> <ref>PMID:12813074</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BACKGROUND: While copper has essential functions as an enzymatic co-factor, excess copper ions are toxic for cells, necessitating mechanisms for regulating its levels. The cusCBFA operon of E. coli encodes a four-component efflux pump dedicated to the extrusion of Cu(I) and Ag(I) ions. METHODOLOGY/PRINCIPAL FINDINGS: We have solved the X-ray crystal structure of CusC, the outer membrane component of the Cus heavy metal efflux pump, to 2.3 A resolution. The structure has the largest extracellular opening of any outer membrane factor (OMF) protein and suggests, for the first time, the presence of a tri-acylated N-terminal lipid anchor. CONCLUSIONS/SIGNIFICANCE: The CusC protein does not have any obvious features that would make it specific for metal ions, suggesting that the narrow substrate specificity of the pump is provided by other components of the pump, most likely by the inner membrane component CusA.
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Crystal Structure of Escherichia coli CusC, the Outer Membrane Component of a Heavy Metal Efflux Pump.,Kulathila R, Kulathila R, Indic M, van den Berg B PLoS One. 2011 Jan 7;6(1):e15610. PMID:21249122<ref>PMID:21249122</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 3pik" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Berg, B van den]]
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[[Category: Van den Berg B]]
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[[Category: Beta-barrel]]
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[[Category: Heavy metal efflux pump]]
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[[Category: Lipoprotein]]
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[[Category: Modified at the n-terminus with diacylglycerol and palmitate]]
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[[Category: Outer membrane]]
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[[Category: Transport protein]]
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Revision as of 13:31, 1 March 2024

Outer membrane protein CusC

PDB ID 3pik

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