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| | <StructureSection load='3zg1' size='340' side='right'caption='[[3zg1]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='3zg1' size='340' side='right'caption='[[3zg1]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zg1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupmc Cupmc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZG1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zg1]] is a 4 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=3ZG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZG1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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]] 1.85Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2y39|2y39]], [[2y3b|2y3b]], [[2y3d|2y3d]], [[2y3g|2y3g]], [[2y3h|2y3h]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></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=3zg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zg1 OCA], [https://pdbe.org/3zg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zg1 RCSB], [https://www.ebi.ac.uk/pdbsum/3zg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zg1 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=3zg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zg1 OCA], [https://pdbe.org/3zg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zg1 RCSB], [https://www.ebi.ac.uk/pdbsum/3zg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zg1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CNRR_RALME CNRR_RALME]] CnrH alone is able to activate cnr expression, while both CnrY and CrnR (CnrX) are needed for nickel induction of CnrH (PubMed:10671463). Has been suggested (PubMed:10671464) to bind nickel.
| + | [https://www.uniprot.org/uniprot/CNRR_CUPMC CNRR_CUPMC] CnrH alone is able to activate cnr expression, while both CnrY and CrnR (CnrX) are needed for nickel induction of CnrH (PubMed:10671463). Has been suggested (PubMed:10671464) to bind nickel.<ref>PMID:10671463</ref> <ref>PMID:10671464</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cupmc]] | + | [[Category: Cupriavidus metallidurans CH34]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Coves, J]] | + | [[Category: Coves J]] |
| - | [[Category: Girard, E]] | + | [[Category: Girard E]] |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Sensor protein]]
| + | |
| - | [[Category: Signal transduction]]
| + | |
| Structural highlights
3zg1 is a 4 chain structure with sequence from Cupriavidus metallidurans CH34. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.85Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
CNRR_CUPMC CnrH alone is able to activate cnr expression, while both CnrY and CrnR (CnrX) are needed for nickel induction of CnrH (PubMed:10671463). Has been suggested (PubMed:10671464) to bind nickel.[1] [2]
Publication Abstract from PubMed
When CnrX, the periplasmic sensor protein in the CnrYXH transmembrane signal transduction complex of Cupriavidus metallidurans CH34, binds the cognate metal ions Ni(ii) or Co(ii), the ECF-type sigma factor CnrH is made available in the cytoplasm for the RNA-polymerase to initiate transcription at the cnrYp and cnrCp promoters. Ni(ii) or Co(ii) are sensed by a metal-binding site with a N3O2S coordination sphere with octahedral geometry, where S stands for the thioether sulfur of the only methionine (Met123) residue of CnrX. The M123A-CnrX derivative has dramatically reduced signal propagation in response to metal sensing while the X-ray structure of Ni-bound M123A-CnrXs showed that the metal-binding site was not affected by the mutation. Ni(ii) remained six-coordinate in M123A-CnrXs, with a water molecule replacing the sulfur as the sixth ligand. H32A-CnrXs, the soluble model of the wild-type membrane-anchored CnrX, was compared to the double mutants H32A-M123A-CnrXs and H32A-M123C-CnrXs to spectroscopically evaluate the role of this unique ligand in the binding site of Ni or Co. The Co- and Ni-bound forms of the protein display unusually blue-shifted visible spectra. TD-DFT calculations using structure-based models allowed identification and assignment of the electronic transitions of Co-bound form of the protein and its M123A derivative. Among them, the signature of the S-Co transition is distinguishable in the shoulder at 530 nm. In vitro affinity measurements point out the crucial role of Met123 in the selectivity for Ni or Co, and in vivo data support the conclusion that Met123 is a trigger of the signal transduction.
Metal sensing and signal transduction by CnrX from Cupriavidus metallidurans CH34: role of the only methionine assessed by a functional, spectroscopic, and theoretical study.,Trepreau J, Grosse C, Mouesca JM, Sarret G, Girard E, Petit-Haertlein I, Kuennemann S, Desbourdes C, de Rosny E, Maillard AP, Nies DH, Coves J Metallomics. 2013 Oct 23. PMID:24154823[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Grass G, Grosse C, Nies DH. Regulation of the cnr cobalt and nickel resistance determinant from Ralstonia sp. strain CH34. J Bacteriol. 2000 Mar;182(5):1390-8. PMID:10671463
- ↑ Tibazarwa C, Wuertz S, Mergeay M, Wyns L, van Der Lelie D. Regulation of the cnr cobalt and nickel resistance determinant of Ralstonia eutropha (Alcaligenes eutrophus) CH34. J Bacteriol. 2000 Mar;182(5):1399-409. PMID:10671464
- ↑ Trepreau J, Grosse C, Mouesca JM, Sarret G, Girard E, Petit-Haertlein I, Kuennemann S, Desbourdes C, de Rosny E, Maillard AP, Nies DH, Coves J. Metal sensing and signal transduction by CnrX from Cupriavidus metallidurans CH34: role of the only methionine assessed by a functional, spectroscopic, and theoretical study. Metallomics. 2013 Oct 23. PMID:24154823 doi:http://dx.doi.org/10.1039/c3mt00248a
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