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| | ==Crystal structure of apo copper resistance protein CopK== | | ==Crystal structure of apo copper resistance protein CopK== |
| - | <StructureSection load='3dsp' size='340' side='right' caption='[[3dsp]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='3dsp' size='340' side='right'caption='[[3dsp]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3dsp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cupriavidus_metallidurans_ch34 Cupriavidus metallidurans ch34]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DSP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DSP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3dsp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_metallidurans_CH34 Cupriavidus metallidurans CH34]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DSP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DSP FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2k0q|2k0q]], [[3dso|3dso]]</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]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">copK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266264 Cupriavidus metallidurans CH34])</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=3dsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dsp OCA], [https://pdbe.org/3dsp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dsp RCSB], [https://www.ebi.ac.uk/pdbsum/3dsp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dsp ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dsp OCA], [http://pdbe.org/3dsp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dsp RCSB], [http://www.ebi.ac.uk/pdbsum/3dsp PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/COPK_RALME COPK_RALME]] Involved in resistance to copper. Can bind up to 2 copper ions. Has higher affinity for Cu(+) than for Cu(2+).<ref>PMID:18533181</ref> | + | [https://www.uniprot.org/uniprot/COPK_CUPMC COPK_CUPMC] Involved in resistance to copper. Can bind up to 2 copper ions. Has higher affinity for Cu(+) than for Cu(2+).<ref>PMID:18533181</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ds/3dsp_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ds/3dsp_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cupriavidus metallidurans ch34]] | + | [[Category: Cupriavidus metallidurans CH34]] |
| - | [[Category: Ash, M R]] | + | [[Category: Large Structures]] |
| - | [[Category: Maher, M J]] | + | [[Category: Ash M-R]] |
| - | [[Category: Copper binding]] | + | [[Category: Maher MJ]] |
| - | [[Category: Copper resistance]]
| + | |
| - | [[Category: Metal binding protein]]
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| Structural highlights
Function
COPK_CUPMC Involved in resistance to copper. Can bind up to 2 copper ions. Has higher affinity for Cu(+) than for Cu(2+).[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 bacterium Cupriavidus metallidurans CH34 is resistant to high environmental concentrations of many metal ions, including copper. This ability arises primarily from the presence of a large plasmid pMOL30 which includes a cluster of 19 cop genes that respond to copper. One of the protein products CopK is induced at high levels and is expressed to the periplasm as a small soluble protein (8.3 kDa). Apo-CopK associates in solution to form a dimer (K(D) approximately 10(-5) M) whose structure was defined by NMR and X-ray crystallography. The individual molecules feature two antiparallel beta-sheets arranged in a sandwich-like structure and interact through C-terminal beta-strands. It binds Cu(II) with low affinity (K(D)(Cu(II)) > 10(-6) M) but Cu(I) with high affinity (K(D)(Cu(I)) = 2 x 10(-11) M). Cu(I)-CopK was also a dimer in the solid state and featured a distorted tetrahedral site Cu(I)(S-Met)(3)(NCS). The isothiocyanato ligand originated from the crystallization solution. Binding of Cu(I) or Ag(I), but not of Cu(II), favored the monomeric form in solution. While Ag(I)-CopK was stable as isolated, Cu(I)-CopK was moderately air-sensitive due to a strong binding cooperativity between Cu(I) and Cu(II). This was documented by determination of the Cu(I) and Cu(II) binding affinities in the presence of the other ion: K(D)(Cu(I)) = 2 x 10(-13) M and K(D)(Cu(II)) = 3 x 10(-12) M, that is, binding of Cu(II) increased the affinity for Cu(I) by a factor of approximately 10(2) and binding of Cu(I) increased the affinity for Cu(II) by a factor of at least 10(6). Stable forms of both Cu(I)Cu(II)-CopK and Ag(I)Cu(II)-CopK were isolated readily. Consistent with this unprecedented copper binding chemistry, NMR spectroscopy detected three distinct forms: apo-CopK, Cu(I)-CopK and Cu(I)Cu(II)-CopK that do not exchange on the NMR time scale. This information provides a valuable guide to the role of CopK in copper resistance.
Unprecedented Binding Cooperativity between Cu(I) and Cu(II) in the Copper Resistance Protein CopK from Cupriavidus metallidurans CH34: Implications from Structural Studies by NMR Spectroscopy and X-Ray Crystallography.,Chong LX, Ash MR, Maher MJ, Hinds MG, Xiao Z, Wedd AG J Am Chem Soc. 2009 Feb 24. PMID:19236095[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bersch B, Favier A, Schanda P, van Aelst S, Vallaeys T, Coves J, Mergeay M, Wattiez R. Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge. J Mol Biol. 2008 Jul 4;380(2):386-403. Epub 2008 May 15. PMID:18533181 doi:10.1016/j.jmb.2008.05.017
- ↑ Chong LX, Ash MR, Maher MJ, Hinds MG, Xiao Z, Wedd AG. Unprecedented Binding Cooperativity between Cu(I) and Cu(II) in the Copper Resistance Protein CopK from Cupriavidus metallidurans CH34: Implications from Structural Studies by NMR Spectroscopy and X-Ray Crystallography. J Am Chem Soc. 2009 Feb 24. PMID:19236095 doi:10.1021/ja807354z
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