2gcf
From Proteopedia
(New page: 200px<br /><applet load="2gcf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gcf" /> '''Solution structure of the N-terminal domain ...) |
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'''Solution structure of the N-terminal domain of the coppper(I) ATPase PacS in its apo form'''<br /> | '''Solution structure of the N-terminal domain of the coppper(I) ATPase PacS in its apo form'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The thylakoid compartments of plant chloroplasts are a vital destination | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 2GCF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full crystallographic information is available from [http:// | + | 2GCF is a [http://en.wikipedia.org/wiki/Single_protein 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]. |
==Reference== | ==Reference== | ||
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[[Category: Bertini, I.]] | [[Category: Bertini, I.]] | ||
[[Category: Ciofi-Baffoni, S.]] | [[Category: Ciofi-Baffoni, S.]] | ||
| - | [[Category: Kandias, N | + | [[Category: Kandias, N G.]] |
| - | [[Category: Robinson, N | + | [[Category: Robinson, N J.]] |
| - | [[Category: SPINE, Structural | + | [[Category: SPINE, Structural Proteomics in Europe.]] |
| - | [[Category: Spyroulias, G | + | [[Category: Spyroulias, G A.]] |
[[Category: ferredoxin-like fold; beta-alpha-beta-beta-alpha-beta]] | [[Category: ferredoxin-like fold; beta-alpha-beta-beta-alpha-beta]] | ||
[[Category: spine]] | [[Category: spine]] | ||
| Line 25: | Line 25: | ||
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:30:22 2008'' |
Revision as of 15:30, 21 February 2008
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Solution structure of the N-terminal domain of the coppper(I) ATPase PacS in its apo form
Overview
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.
About this Structure
2GCF is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 17:30:22 2008
Categories: Single protein | Synechocystis sp. | Banci, L. | Bertini, I. | Ciofi-Baffoni, S. | Kandias, N G. | Robinson, N J. | SPINE, Structural Proteomics in Europe. | Spyroulias, G A. | Ferredoxin-like fold; beta-alpha-beta-beta-alpha-beta | Spine | Structural genomics | Structural proteomics in europe
