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| | <StructureSection load='3e6z' size='340' side='right'caption='[[3e6z]], [[Resolution|resolution]] 1.00Å' scene=''> | | <StructureSection load='3e6z' size='340' side='right'caption='[[3e6z]], [[Resolution|resolution]] 1.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3e6z]] 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=3E6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E6Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3e6z]] 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=3E6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E6Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zeq|1zeq]], [[2qcp|2qcp]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cusF, cusX, ylcC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=3e6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6z OCA], [https://pdbe.org/3e6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e6z RCSB], [https://www.ebi.ac.uk/pdbsum/3e6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e6z 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=3e6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e6z OCA], [https://pdbe.org/3e6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e6z RCSB], [https://www.ebi.ac.uk/pdbsum/3e6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e6z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CUSF_ECOLI CUSF_ECOLI]] Part of a cation efflux system that mediates resistance to copper and silver. Binds one copper per polypeptide.<ref>PMID:11399769</ref>
| + | [https://www.uniprot.org/uniprot/CUSF_ECOLI CUSF_ECOLI] Part of a cation efflux system that mediates resistance to copper and silver. Binds one copper per polypeptide.<ref>PMID:11399769</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Loftin, I R]] | + | [[Category: Loftin IR]] |
| - | [[Category: Beta-barrel]]
| + | |
| - | [[Category: Copper chaperone]]
| + | |
| - | [[Category: Copper-binding]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Metal resistance]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Metalloprotein]]
| + | |
| - | [[Category: Ob-fold]]
| + | |
| - | [[Category: Periplasm]]
| + | |
| Structural highlights
Function
CUSF_ECOLI Part of a cation efflux system that mediates resistance to copper and silver. Binds one copper per polypeptide.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The periplasmic metallochaperone CusF coordinates Cu(I) and Ag(I) through a unique site consisting of a Met(2)His motif as well as a Cu(I)-pi interaction between a nearby tryptophan, W44, and the metal ion. Through mutational analyses we investigate here the role that W44 in CusF plays in metal coordination. Nuclear magnetic resonance spectra show that the specificity of CusF for Cu(I) and Ag(I) is not altered by mutation of W44. X-ray absorption spectroscopy studies reveal that W44 protects the bound Cu(I) from oxidation as well as from adventitious ligands. Competition assays demonstrate that W44 does not significantly contribute to the affinity of CusF for metal, but that substitution of W44 by methionine, which forms a fourth Cu(I) ligand, substantially increases the affinity. These studies indicate that W44 is important in maintaining a moderate-affinity and solvent-shielded three-coordinate environment for Cu(I), which has implications for the function of CusF as a metallochaperone.
Tryptophan Cu(I)-pi interaction fine-tunes the metal binding properties of the bacterial metallochaperone CusF.,Loftin IR, Blackburn NJ, McEvoy MM J Biol Inorg Chem. 2009 Apr 21. PMID:19381697[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Outten FW, Huffman DL, Hale JA, O'Halloran TV. The independent cue and cus systems confer copper tolerance during aerobic and anaerobic growth in Escherichia coli. J Biol Chem. 2001 Aug 17;276(33):30670-7. Epub 2001 Jun 8. PMID:11399769 doi:http://dx.doi.org/10.1074/jbc.M104122200
- ↑ Loftin IR, Blackburn NJ, McEvoy MM. Tryptophan Cu(I)-pi interaction fine-tunes the metal binding properties of the bacterial metallochaperone CusF. J Biol Inorg Chem. 2009 Apr 21. PMID:19381697 doi:10.1007/s00775-009-0503-y
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