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| {{STRUCTURE_2gcf| PDB=2gcf | SCENE= }} | | {{STRUCTURE_2gcf| PDB=2gcf | SCENE= }} |
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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=== |
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| ==Overview==
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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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16707580}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16707580 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16707580}} |
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| ==About this Structure== | | ==About this Structure== |
| 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]. | | 2GCF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GCF OCA]. |
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| ==Reference== | | ==Reference== |
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| [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| [[Category: Structural proteomics in europe]] | | [[Category: Structural proteomics in europe]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:19:36 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:32:37 2008'' |
