2gcf: Difference between revisions

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[[Image:2gcf.gif|left|200px]]


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==Solution structure of the N-terminal domain of the coppper(I) ATPase PacS in its apo form==
The line below this paragraph, containing "STRUCTURE_2gcf", creates the "Structure Box" on the page.
<StructureSection load='2gcf' size='340' side='right'caption='[[2gcf]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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'>[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>
{{STRUCTURE_2gcf| PDB=2gcf |  SCENE= }}
</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: Beta-alpha-beta-beta-alpha-beta]]
[[Category: Ferredoxin-like fold]]
[[Category: Spine]]
[[Category: Structural genomic]]
[[Category: Structural proteomics in europe]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:19:36 2008''

Latest revision as of 09:40, 1 May 2024

Solution structure of the N-terminal domain of the coppper(I) ATPase PacS in its apo formSolution structure of the N-terminal domain of the coppper(I) ATPase PacS in its apo form

Structural highlights

2gcf is a 1 chain structure with sequence from Synechocystis sp. PCC 6803. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ATCS_SYNY3 May play a role in the osmotic adaptation (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

Drag the structure with the mouse to rotate

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OCA
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