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| | ==Solution Structure of the N-terminal Domain of a Potential Copper-translocating P-type ATPase from Bacillus subtilis in the Cu(I)loaded State== | | ==Solution Structure of the N-terminal Domain of a Potential Copper-translocating P-type ATPase from Bacillus subtilis in the Cu(I)loaded State== |
| - | <StructureSection load='1kqk' size='340' side='right' caption='[[1kqk]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='1kqk' size='340' side='right'caption='[[1kqk]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kqk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KQK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kqk]] 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=1KQK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KQK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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">[[1jww|1jww]]</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">yvgX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</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=1kqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kqk OCA], [https://pdbe.org/1kqk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kqk RCSB], [https://www.ebi.ac.uk/pdbsum/1kqk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kqk ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Copper-exporting_ATPase Copper-exporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.4 3.6.3.4] </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=1kqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kqk OCA], [http://pdbe.org/1kqk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kqk RCSB], [http://www.ebi.ac.uk/pdbsum/1kqk PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/COPA_BACSU COPA_BACSU]] Involved in copper export.<ref>PMID:12644235</ref> | + | [https://www.uniprot.org/uniprot/COPA_BACSU COPA_BACSU] Involved in copper export.<ref>PMID:12644235</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/kq/1kqk_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kq/1kqk_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: Bacillus globigii migula 1900]] | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Copper-exporting ATPase]] | + | [[Category: Large Structures]] |
| - | [[Category: Banci, L]] | + | [[Category: Banci L]] |
| - | [[Category: Bertini, I]] | + | [[Category: Bertini I]] |
| - | [[Category: Ciofi-Baffoni, S]] | + | [[Category: Ciofi-Baffoni S]] |
| - | [[Category: Gonnelli, L]] | + | [[Category: D'Onofrio M]] |
| - | [[Category: Marhuenda-Egea, F C]] | + | [[Category: Gonnelli L]] |
| - | [[Category: Onofrio, M D]] | + | [[Category: Marhuenda-Egea FC]] |
| - | [[Category: Ruiz-Duenas, F J]] | + | [[Category: Ruiz-Duenas FJ]] |
| - | [[Category: Copa]]
| + | |
| - | [[Category: Copper transporting protein]]
| + | |
| - | [[Category: Folding]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: P-type atpase]]
| + | |
| Structural highlights
Function
COPA_BACSU Involved in copper export.[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
A putative partner of the already characterized CopZ from Bacillus subtilis was found, both proteins being encoded by genes located in the same operon. This new protein is highly homologous to eukaryotic and prokaryotic P-type ATPases such as CopA, Ccc2 and Menkes proteins. The N-terminal region of this protein contains two soluble domains constituted by amino acid residues 1 to 72 and 73 to 147, respectively, which were expressed both separately and together. In both cases only the 73-147 domain is folded and is stable both in the copper(I)-free and in the copper(I)-bound forms. The folded and unfolded state is monitored through the chemical shift dispersion of 15N-HSQC spectra. In the absence of any structural characterization of CopA-type proteins, we determined the structure of the 73-147 domain in the 1-151 construct in the apo state through 1H, 15N and 13C NMR spectroscopies. The structure of the Cu(I)-loaded 73-147 domain has been also determined in the construct 73-151. About 1300 meaningful NOEs and 90 dihedral angles were used to obtain structures at high resolution both for the Cu(I)-bound and the Cu(I)-free states (backbone RMSD to the mean 0.35(+/-0.06) A and 0.39(+/-0.07) A, respectively). The structural assessment shows that the structures are accurate. The protein has the typical betaalpha(betabeta)alphabeta folding with a cysteine in the C-terminal part of helix alpha1 and the other cysteine in loop 1. The structures are similar to other proteins involved in copper homeostasis. Particularly, between BsCopA and BsCopZ, only the charges located around loop 1 are reversed for BsCopA and BsCopZ, thus suggesting that the two proteins could interact one with the other. The variability in conformation displayed by the N-terminal cysteine of the CXXC motif in a number of structures of copper transporting proteins suggests that this may be the cysteine which binds first to the copper(I) carried by the partner protein.
Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states.,Banci L, Bertini I, Ciofi-Baffoni S, D'Onofrio M, Gonnelli L, Marhuenda-Egea FC, Ruiz-Duenas FJ J Mol Biol. 2002 Mar 29;317(3):415-29. PMID:11922674[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Radford DS, Kihlken MA, Borrelly GP, Harwood CR, Le Brun NE, Cavet JS. CopZ from Bacillus subtilis interacts in vivo with a copper exporting CPx-type ATPase CopA. FEMS Microbiol Lett. 2003 Mar 14;220(1):105-12. PMID:12644235
- ↑ Banci L, Bertini I, Ciofi-Baffoni S, D'Onofrio M, Gonnelli L, Marhuenda-Egea FC, Ruiz-Duenas FJ. Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded states. J Mol Biol. 2002 Mar 29;317(3):415-29. PMID:11922674 doi:10.1006/jmbi.2002.5430
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