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| | ==Copper trafficking: the solution structure of Bacillus subtilis CopZ== | | ==Copper trafficking: the solution structure of Bacillus subtilis CopZ== |
| - | <StructureSection load='1k0v' size='340' side='right'caption='[[1k0v]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='1k0v' size='340' side='right'caption='[[1k0v]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1k0v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K0V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1k0v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K0V FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1cpz|1cpz]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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">bscopz ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1k0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k0v OCA], [https://pdbe.org/1k0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k0v RCSB], [https://www.ebi.ac.uk/pdbsum/1k0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k0v 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=1k0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k0v OCA], [https://pdbe.org/1k0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k0v RCSB], [https://www.ebi.ac.uk/pdbsum/1k0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k0v ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/COPZ_BACSU COPZ_BACSU]] Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-transporting ATPase CopA.
| + | [https://www.uniprot.org/uniprot/COPZ_BACSU COPZ_BACSU] Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-transporting ATPase CopA. |
| | == 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: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Banci, L]] | + | [[Category: Banci L]] |
| - | [[Category: Bertini, I]] | + | [[Category: Bertini I]] |
| - | [[Category: Conte, R Del]] | + | [[Category: Del Conte R]] |
| - | [[Category: Markey, J]] | + | [[Category: Markey J]] |
| - | [[Category: Ruiz-Duenas, F J]] | + | [[Category: Ruiz-Duenas FJ]] |
| - | [[Category: Beta-alpha-beta-beta-alpha-beta]]
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| - | [[Category: Metal transport]]
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| Structural highlights
Function
COPZ_BACSU Chaperone that serves for the intracellular sequestration and transport of Cu(+). Delivers Cu(+) to the copper-transporting ATPase CopA.
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
A sequence with a high homology (39% residue identity) with that of the copper-transport CopZ protein from Enterococcus hirae and with the same MXCXXC metal-binding motif has been identified in the genome of Bacillus subtilis, and the corresponding protein has been expressed. The protein, constituted by 73 amino acids, does bind copper(I) under reducing conditions and fully folded in both copper-bound and copper-free forms under the present experimental conditions. The solution structure of the copper-bound form was determined through NMR spectroscopy on an 15N-labeled sample. A total of 1508 meaningful nuclear Overhauser effects, 38 dihedral phi angles, and 48 dihedral psi angles were used in the structural calculations, which lead to a family of 30 conformers with an average rmsd to the mean structure of 0.32 +/- 0.06 A for the backbone and of 0.85 +/- 0.07 A for the heavy atoms. NMR data on the apoprotein also show that, also in this form, the protein is in a folded state and essentially maintains the complete secondary structure. Some disorder is observed in the loop devoted to copper binding. These results are compared with those reported for CopZ from E. hirae whose structure is well-defined only in the apo form. The different behaviors of copper-loaded E. hirae and B. subtilis are tentatively accounted for on the basis of the presence of dithiothreitol used in the latter case, which would stabilize the monomeric form. The comparison is extended to other similar proteins, with particular attention to the copper-binding loop. The nature and the location of conserved residues around the metal-binding site are discussed with respect to their relevance for the metal-binding process. Proposals for the role of CopZ are also presented.
Copper trafficking: the solution structure of Bacillus subtilis CopZ.,Banci L, Bertini I, Del Conte R, Markey J, Ruiz-Duenas FJ Biochemistry. 2001 Dec 25;40(51):15660-8. PMID:11747441[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Banci L, Bertini I, Del Conte R, Markey J, Ruiz-Duenas FJ. Copper trafficking: the solution structure of Bacillus subtilis CopZ. Biochemistry. 2001 Dec 25;40(51):15660-8. PMID:11747441
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