2GCF

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

Summary for 2GCF

• Entry DOI: 10.2210/pdb2gcf/pdb
• Descriptor: Cation-transporting ATPase pacS (1 entity in total)
• Functional Keywords: ferredoxin-like fold, beta-alpha-beta-beta-alpha-beta, structural genomics, structural proteomics in europe, spine, hydrolase
• Biological source: Synechocystis sp.
• Cellular location: Cell membrane; Multi-pass membrane protein: P73241
• Total number of polymer chains: 1
• Total formula weight: 7910.03

Authors

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Kandias, N.G.,Spyroulias, G.A.,Robinson, N.J.,Structural Proteomics in Europe (SPINE) (deposition date: 2006-03-14, release date: 2006-05-30, Last modification date: 2024-05-01)

Primary citation

Banci, L.,Bertini, I.,Ciofi-Baffoni, S.,Kandias, N.G.,Robinson, N.J.,Spyroulias, G.A.,Su, X.C.,Tottey, S.,Vanarotti, M.
The delivery of copper for thylakoid import observed by NMR.
Proc.Natl.Acad.Sci.Usa, 103:8320-8325, 2006

PubMed Abstract: 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.

PubMed: 16707580
DOI: 10.1073/pnas.0600142103

Experimental method

SOLUTION NMR