|
|
| (15 intermediate revisions by the same user not shown) |
| Line 1: |
Line 1: |
| [[Image:2gcf.gif|left|200px]]
| |
|
| |
|
| {{Structure
| | ==Solution structure of the N-terminal domain of the coppper(I) ATPase PacS in its apo form== |
| |PDB= 2gcf |SIZE=350|CAPTION= <scene name='initialview01'>2gcf</scene>
| | <StructureSection load='2gcf' size='340' side='right'caption='[[2gcf]]' scene=''> |
| |SITE= | | == Structural highlights == |
| |LIGAND=
| | <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> |
| |ACTIVITY=
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| |GENE= pacS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.])
| | <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> |
| | == Function == |
| | [https://www.uniprot.org/uniprot/ATCS_SYNY3 ATCS_SYNY3] May play a role in the osmotic adaptation (By similarity). |
| | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> |
| | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gc/2gcf_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> |
| | </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> |
|
| |
|
| '''Solution structure of the N-terminal domain of the coppper(I) ATPase PacS in its apo form'''
| | ==See Also== |
| | | *[[ATPase 3D structures|ATPase 3D structures]] |
| | | __TOC__ |
| ==Overview== | | </StructureSection> |
| 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.
| | [[Category: Large Structures]] |
| | | [[Category: Synechocystis sp. PCC 6803]] |
| ==About this Structure==
| | [[Category: Banci L]] |
| 2GCF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GCF OCA].
| | [[Category: Bertini I]] |
| | | [[Category: Ciofi-Baffoni S]] |
| ==Reference==
| | [[Category: Kandias NG]] |
| 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:[http://www.ncbi.nlm.nih.gov/pubmed/16707580 16707580]
| | [[Category: Robinson NJ]] |
| [[Category: Single protein]] | | [[Category: Spyroulias GA]] |
| [[Category: Synechocystis sp.]] | |
| [[Category: Banci, L.]] | |
| [[Category: Bertini, I.]] | |
| [[Category: Ciofi-Baffoni, S.]] | |
| [[Category: Kandias, N G.]] | |
| [[Category: Robinson, N J.]] | |
| [[Category: SPINE, Structural Proteomics in Europe.]]
| |
| [[Category: Spyroulias, G A.]] | |
| [[Category: ferredoxin-like fold; beta-alpha-beta-beta-alpha-beta]]
| |
| [[Category: spine]]
| |
| [[Category: structural genomic]]
| |
| [[Category: structural proteomics in europe]]
| |
| | |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:03:05 2008''
| |