2gcf: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: left|200px<br /><applet load="2gcf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gcf" /> '''Solution structure of the N-terminal domain ... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2gcf.gif|left|200px]]<br /><applet load="2gcf" size=" | [[Image:2gcf.gif|left|200px]]<br /><applet load="2gcf" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2gcf" /> | caption="2gcf" /> | ||
'''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== | ||
| Line 16: | Line 16: | ||
[[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'' | ||
