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| | <StructureSection load='2vb3' size='340' side='right'caption='[[2vb3]], [[Resolution|resolution]] 2.33Å' scene=''> | | <StructureSection load='2vb3' size='340' side='right'caption='[[2vb3]], [[Resolution|resolution]] 2.33Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vb3]] is a 1 chain structure with sequence from [http://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=2VB3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VB3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vb3]] 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=2VB3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VB3 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></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]] 2.33Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zeq|1zeq]], [[2vb2|2vb2]]</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></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2vb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vb3 OCA], [http://pdbe.org/2vb3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vb3 RCSB], [http://www.ebi.ac.uk/pdbsum/2vb3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vb3 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=2vb3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vb3 OCA], [https://pdbe.org/2vb3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vb3 RCSB], [https://www.ebi.ac.uk/pdbsum/2vb3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vb3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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: Balakrishnan, G]] | + | [[Category: Balakrishnan G]] |
| - | [[Category: Davis, A V]] | + | [[Category: Davis AV]] |
| - | [[Category: Focia, P]] | + | [[Category: Focia P]] |
| - | [[Category: Halloran, T V.O]] | + | [[Category: O'Halloran TV]] |
| - | [[Category: Penner-Hahn, J E]] | + | [[Category: Penner-Hahn JE]] |
| - | [[Category: Spiro, T G]] | + | [[Category: Spiro TG]] |
| - | [[Category: Staehlin, B M]] | + | [[Category: Staehlin BM]] |
| - | [[Category: Stasser, J P]] | + | [[Category: Stasser JP]] |
| - | [[Category: Xue, Y]] | + | [[Category: Xue Y]] |
| - | [[Category: Cation pi]]
| + | |
| - | [[Category: Copper tolerance]]
| + | |
| - | [[Category: Copper transport]]
| + | |
| - | [[Category: Metal transport]]
| + | |
| - | [[Category: Metal-binding]]
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| 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
Methionine-rich motifs have an important role in copper trafficking factors, including the CusF protein. Here we show that CusF uses a new metal recognition site wherein Cu(I) is tetragonally displaced from a Met2His ligand plane toward a conserved tryptophan. Spectroscopic studies demonstrate that both thioether ligation and strong cation-pi interactions with tryptophan stabilize metal binding. This novel active site chemistry affords mechanisms for control of adventitious metal redox and substitution chemistry.
Cu(I) recognition via cation-pi and methionine interactions in CusF.,Xue Y, Davis AV, Balakrishnan G, Stasser JP, Staehlin BM, Focia P, Spiro TG, Penner-Hahn JE, O'Halloran TV Nat Chem Biol. 2008 Feb;4(2):107-9. Epub 2007 Dec 23. PMID:18157124[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
- ↑ Xue Y, Davis AV, Balakrishnan G, Stasser JP, Staehlin BM, Focia P, Spiro TG, Penner-Hahn JE, O'Halloran TV. Cu(I) recognition via cation-pi and methionine interactions in CusF. Nat Chem Biol. 2008 Feb;4(2):107-9. Epub 2007 Dec 23. PMID:18157124 doi:10.1038/nchembio.2007.57
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