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| ==Solution structure of the N-terminal domain of the coppper(I) ATPase PacS in its apo form== | | ==Solution structure of the N-terminal domain of the coppper(I) ATPase PacS in its apo form== |
| <StructureSection load='2gcf' size='340' side='right' caption='[[2gcf]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''> | | <StructureSection load='2gcf' size='340' side='right'caption='[[2gcf]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[2gcf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GCF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GCF FirstGlance]. <br> | | <table><tr><td colspan='2'>[[2gcf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GCF FirstGlance]. <br> |
| </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pacS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1148 Aphanocapsa sp. (strain N-1)])</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='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=2gcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gcf OCA], [http://pdbe.org/2gcf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gcf RCSB], [http://www.ebi.ac.uk/pdbsum/2gcf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gcf 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=2gcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gcf OCA], [https://pdbe.org/2gcf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gcf RCSB], [https://www.ebi.ac.uk/pdbsum/2gcf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gcf ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/ATCS_SYNY3 ATCS_SYNY3]] May play a role in the osmotic adaptation (By similarity). | | [https://www.uniprot.org/uniprot/ATCS_SYNY3 ATCS_SYNY3] May play a role in the osmotic adaptation (By similarity). |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gcf ConSurf]. | | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gcf ConSurf]. |
| <div style="clear:both"></div> | | <div style="clear:both"></div> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The thylakoid compartments of plant chloroplasts are a vital destination for copper. Copper is needed to form holo-plastocyanin, which must shuttle electrons between photosystems to convert light into biologically useful chemical energy. Copper can bind tightly to proteins, so it has been hypothesized that copper partitions onto ligand-exchange pathways to reach intracellular locations without inflicting damage en route. The copper metallochaperone Atx1 of chloroplast-related cyanobacteria (ScAtx1) engages in bacterial two-hybrid interactions with N-terminal domains of copper-transporting ATPases CtaA (cell import) and PacS (thylakoid import). Here we visualize copper delivery. The N-terminal domain PacS(N) has a ferredoxin-like fold that forms copper-dependent heterodimers with ScAtx1. Removal of copper, by the addition of the cuprous-ion chelator bathocuproine disulfonate, disrupts this heterodimer, as shown from a reduction of the overall tumbling rate of the protein mixture. The NMR spectral changes of the heterodimer versus the separate proteins reveal that loops 1, 3, and 5 (the carboxyl tail) of the ScAtx1 Cu(I) site switch to an apo-like configuration in the heterodimer. NMR data ((2)J(NH) couplings in the imidazole ring of (15)N ScAtx1 His-61) also show that His-61, bound to copper(I) in [Cu(I)ScAtx1](2), is not coordinated to copper in the heterodimer. A model for the PacS(N)/Cu(I)/ScAtx1 complex is presented. Contact with PacS(N) induces change to the ScAtx1 copper-coordination sphere that drives copper release for thylakoid import. These data also elaborate on the mechanism to keep copper(I) out of the ZiaA(N) ATPase zinc sites.
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| The delivery of copper for thylakoid import observed by NMR.,Banci L, Bertini I, Ciofi-Baffoni S, Kandias NG, Robinson NJ, Spyroulias GA, Su XC, Tottey S, Vanarotti M Proc Natl Acad Sci U S A. 2006 May 30;103(22):8320-5. Epub 2006 May 17. PMID:16707580<ref>PMID:16707580</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 2gcf" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[ATPase|ATPase]] | | *[[ATPase 3D structures|ATPase 3D structures]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Banci, L]] | | [[Category: Large Structures]] |
| [[Category: Bertini, I]] | | [[Category: Synechocystis sp. PCC 6803]] |
| [[Category: Ciofi-Baffoni, S]] | | [[Category: Banci L]] |
| [[Category: Kandias, N G]] | | [[Category: Bertini I]] |
| [[Category: Robinson, N J]] | | [[Category: Ciofi-Baffoni S]] |
| [[Category: SPINE, Structural Proteomics in Europe]]
| | [[Category: Kandias NG]] |
| [[Category: Spyroulias, G A]]
| | [[Category: Robinson NJ]] |
| [[Category: Beta-alpha-beta-beta-alpha-beta]]
| | [[Category: Spyroulias GA]] |
| [[Category: Ferredoxin-like fold]] | |
| [[Category: Hydrolase]] | |
| [[Category: Spine]] | |
| [[Category: Structural genomic]]
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| [[Category: Structural proteomics in europe]]
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