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| | <StructureSection load='2qcp' size='340' side='right'caption='[[2qcp]], [[Resolution|resolution]] 1.00Å' scene=''> | | <StructureSection load='2qcp' size='340' side='right'caption='[[2qcp]], [[Resolution|resolution]] 1.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2qcp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecow3 Ecow3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QCP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2qcp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._W3110 Escherichia coli str. K-12 substr. W3110]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QCP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AG:SILVER+ION'>AG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AG:SILVER+ION'>AG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cusF, cusX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316407 ECOW3])</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=2qcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qcp OCA], [https://pdbe.org/2qcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qcp RCSB], [https://www.ebi.ac.uk/pdbsum/2qcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qcp 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=2qcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qcp OCA], [https://pdbe.org/2qcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qcp RCSB], [https://www.ebi.ac.uk/pdbsum/2qcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qcp 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: Ecow3]] | + | [[Category: Escherichia coli str. K-12 substr. W3110]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Loftin, I R]] | + | [[Category: Loftin IR]] |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: Copper-binding]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Metal resistance]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Metalloprotein]]
| + | |
| - | [[Category: Ob-fold]]
| + | |
| - | [[Category: Periplasmic]]
| + | |
| - | [[Category: Silver-binding]]
| + | |
| 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
Elevated levels of copper or silver ions in the environment are an immediate threat to many organisms. Escherichia coli is able to resist the toxic effects of these ions through strictly limiting intracellular levels of Cu(I) and Ag(I). The CusCFBA system is one system in E. coli responsible for copper/silver tolerance. A key component of this system is the periplasmic copper/silver-binding protein, CusF. Here the X-ray structure and XAS data on the CusF-Ag(I) and CusF-Cu(I) complexes, respectively, are reported. In the CusF-Ag(I) structure, Ag(I) is coordinated by two methionines and a histidine, with a nearby tryptophan capping the metal site. EXAFS measurements on the CusF-Cu(I) complex show a similar environment for Cu(I). The arrangement of ligands effectively sequesters the metal from its periplasmic environment and thus may play a role in protecting the cell from the toxic ion.
Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy.,Loftin IR, Franke S, Blackburn NJ, McEvoy MM Protein Sci. 2007 Oct;16(10):2287-93. PMID:17893365[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, Franke S, Blackburn NJ, McEvoy MM. Unusual Cu(I)/Ag(I) coordination of Escherichia coli CusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopy. Protein Sci. 2007 Oct;16(10):2287-93. PMID:17893365 doi:16/10/2287
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