|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Structure of Cu(I)Cu(II)-CopK from Cupriavidus metallidurans CH34== | | ==Structure of Cu(I)Cu(II)-CopK from Cupriavidus metallidurans CH34== |
| - | <StructureSection load='2lel' size='340' side='right'caption='[[2lel]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lel' size='340' side='right'caption='[[2lel]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lel]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupmc Cupmc]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LEL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2lel]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_metallidurans_CH34 Cupriavidus metallidurans CH34]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LEL FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">copK, Rmet_6108 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266264 CUPMC])</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=2lel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lel OCA], [https://pdbe.org/2lel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lel RCSB], [https://www.ebi.ac.uk/pdbsum/2lel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lel 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=2lel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lel OCA], [https://pdbe.org/2lel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lel RCSB], [https://www.ebi.ac.uk/pdbsum/2lel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lel ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cupmc]] | + | [[Category: Cupriavidus metallidurans CH34]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chong, L X]] | + | [[Category: Chong LX]] |
| - | [[Category: Hinds, M G]] | + | [[Category: Hinds MG]] |
| - | [[Category: Wedd, A G]] | + | [[Category: Wedd AG]] |
| - | [[Category: Xiao, Z]] | + | [[Category: Xiao Z]] |
| - | [[Category: Binding cooperativity]]
| + | |
| - | [[Category: Copper protein]]
| + | |
| - | [[Category: Copper resistance]]
| + | |
| - | [[Category: Copper transport]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| 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]
Publication Abstract from PubMed
The bacterium Cupriavidus metallidurans CH34 is resistant to high environmental concentrations of many metal ions. Upon copper challenge, it upregulates the periplasmic protein CopK (8.3 kDa). The function of CopK in the copper resistance response is ill-defined, but CopK demonstrates an intriguing cooperativity: occupation of a high-affinity Cu(I) binding site generates a high-affinity Cu(II) binding site, and the high-affinity Cu(II) binding enhances Cu(I) binding. Native CopK and targeted variants were examined by chromatographic, spectroscopic, and X-ray crystallographic probes. Structures of two distinct forms of Cu(I)Cu(II)-CopK were defined, and structural changes associated with occupation of the Cu(II) site were demonstrated. In solution, monomeric Cu(I)Cu(II)-CopK features the previously elucidated Cu(I) site in Cu(I)-CopK, formed from four S(delta) atoms of Met28, -38, -44, and -54 (site 4S). Binding of Cu(I) to apo-CopK induces a conformational change that releases the C-terminal beta-strand from the beta-sandwich structure. In turn, this allows His70 and N-terminal residues to form a large loop that includes the Cu(II) binding site. In crystals, a polymeric form of Cu(I)Cu(II)-CopK displays a Cu(I) site defined by the S(delta) atoms of Met26, -38, and -54 (site 3S) and an exogenous ligand (modeled as H(2)O) and a Cu(II) site that bridges dimeric CopK molecules. The 3S Cu(I) binding mode observed in crystals was demonstrated in solution in protein variant M44L where site 4S is disabled. The intriguing copper binding chemistry of CopK provides molecular insight into Cu(I) transfer processes. The adaptable nature of the Cu(I) coordination sphere in methionine-rich clusters allows copper to be relayed between clusters during transport across membranes in molecular pumps such as CusA and Ctr1.
Molecular basis of the cooperative binding of Cu(I) and Cu(II) to the CopK protein from Cupriavidus metallidurans CH34.,Ash MR, Chong LX, Maher MJ, Hinds MG, Xiao Z, Wedd AG Biochemistry. 2011 Nov 1;50(43):9237-47. Epub 2011 Oct 4. PMID:21936507[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
- ↑ Ash MR, Chong LX, Maher MJ, Hinds MG, Xiao Z, Wedd AG. Molecular basis of the cooperative binding of Cu(I) and Cu(II) to the CopK protein from Cupriavidus metallidurans CH34. Biochemistry. 2011 Nov 1;50(43):9237-47. Epub 2011 Oct 4. PMID:21936507 doi:10.1021/bi200841f
|
