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| | ==Structure characterization of the water soluble region of P-type ATPase CopA from Bacillus subtilis== | | ==Structure characterization of the water soluble region of P-type ATPase CopA from Bacillus subtilis== |
| - | <StructureSection load='1p6t' size='340' side='right' caption='[[1p6t]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''> | + | <StructureSection load='1p6t' size='340' side='right'caption='[[1p6t]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1p6t]] is a 1 chain structure with sequence from [http://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=1P6T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P6T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1p6t]] 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=1P6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P6T FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1oq3|1oq3]], [[1kqk|1kqk]]</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='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 "Vibrio subtilis" Ehrenberg 1835])</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=1p6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p6t OCA], [https://pdbe.org/1p6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p6t RCSB], [https://www.ebi.ac.uk/pdbsum/1p6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p6t 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=1p6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p6t OCA], [http://pdbe.org/1p6t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p6t RCSB], [http://www.ebi.ac.uk/pdbsum/1p6t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p6t ProSAT]</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]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[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: Gonnelli L]] |
| - | [[Category: SPINE, Structural Proteomics in Europe]]
| + | [[Category: Su XC]] |
| - | [[Category: Su, X C]] | + | |
| - | [[Category: Beta-alpha-beta-beta-alpha-beta fold]]
| + | |
| - | [[Category: Copa]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nmr]]
| + | |
| - | [[Category: P-type atpase]]
| + | |
| - | [[Category: Spine]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Structural proteomics in europe]]
| + | |
| - | [[Category: Water-soluble region]]
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| 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
The solution structure of the N-terminal region (151 amino acids) of a copper ATPase, CopA, from Bacillus subtilis, is reported here. It consists of two domains, CopAa and CopAb, linked by two amino acids. It is found that the two domains, which had already been separately characterized, interact one to the other through a hydrogen bond network and a few hydrophobic interactions, forming a single rigid body. The two metal binding sites are far from one another, and the short link between the domains prevents them from interacting. This and the surface electrostatic potential suggest that each domain receives copper from the copper chaperone, CopZ, independently and transfers it to the membrane binding site of CopA. The affinity constants of silver(I) and copper(I) are similar for the two sites as monitored by NMR. Because the present construct "domain-short link-domain" is shared also by the last two domains of the eukaryotic copper ATPases and several residues at the interface between the two domains are conserved, the conclusions of the present study have general validity for the understanding of the function of copper ATPases.
Structural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilis.,Banci L, Bertini I, Ciofi-Baffoni S, Gonnelli L, Su XC J Biol Chem. 2003 Dec 12;278(50):50506-13. Epub 2003 Sep 27. PMID:14514665[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, Gonnelli L, Su XC. Structural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilis. J Biol Chem. 2003 Dec 12;278(50):50506-13. Epub 2003 Sep 27. PMID:14514665 doi:10.1074/jbc.M307389200
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