Insights into the mechanism of copper transport by the Wilson and Menkes disease copper-transporting ATPases

Fatemi, Negah; Sarkar, Bibudhendra

doi:10.1016/s0020-1693(02)00949-0

Cited by 26 publications

(18 citation statements)

References 77 publications

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“…Our data fit within a model proposed for the function of the Wilson protein in vivo (51,55), where the binding of copper to the domains closest to the transmembrane segments is the first step of the copper transport cycle, sufficient for the basic activity and for the delivery of copper to the multicopper oxidase target. When the copper concentration increases, other metal binding sites become occupied, thus inducing conformational changes that determine the translocation process of the Wilson protein from the transGolgi network to the plasma membrane.…”

Section: Discussionsupporting

confidence: 64%

Structural Basis for the Function of the N-terminal Domain of the ATPase CopA from Bacillus subtilis

Banci

Bertini

Ciofi‐Baffoni

et al. 2003

Journal of Biological Chemistry

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The solution structure of the N-terminal region (151 amino acids) of a copper ATPase, CopA, from Bacillus subtilis, is reported here. It consists of two domains, CopAa and CopAb, linked by two amino acids. It is found that the two domains, which had already been separately characterized, interact one to the other through a hydrogen bond network and a few hydrophobic interactions, forming a single rigid body. The two metal binding sites are far from one another, and the short link between the domains prevents them from interacting. This and the surface electrostatic potential suggest that each domain receives copper from the copper chaperone, CopZ, independently and transfers it to the membrane binding site of CopA. The affinity constants of silver(I) and copper(I) are similar for the two sites as monitored by NMR. Because the present construct "domain-short link-domain" is shared also by the last two domains of the eukaryotic copper ATPases and several residues at the interface between the two domains are conserved, the conclusions of the present study have general validity for the understanding of the function of copper ATPases.

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Section: Discussionsupporting

confidence: 64%

Structural Basis for the Function of the N-terminal Domain of the ATPase CopA from Bacillus subtilis

Banci

Bertini

Ciofi‐Baffoni

et al. 2003

Journal of Biological Chemistry

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“…Fatemi et al presented a model of the overall structure of the Wilson copper ATPase, ATP7B, solely based on sequence similarity to Serca1 (Fatemi and Sarkar 2002). While it was possible to model the large domain from TM3 to TM7 and, individually, the six N-terminal copper-binding domains, their position as well as the positions of TM1, TM2 and TM8 remained unresolved.…”

Section: Discussionmentioning

confidence: 99%

Structural model of the CopA copper ATPase of Enterococcus hirae based on chemical cross-linking

et al. 2008

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The CopA copper ATPase of Enterococcus hirae belongs to the family of heavy metal pumping CPx-type ATPases and shares 43% sequence similarity with the human Menkes and Wilson copper ATPases. Due to a lack of suitable protein crystals, only partial three-dimensional structures have so far been obtained for this family of ion pumps. We present a structural model of CopA derived by combining topological information obtained by intramolecular cross-linking with molecular modeling. Purified CopA was crosslinked with different bivalent reagents, followed by tryptic digestion and identification of cross-linked peptides by mass spectrometry. The structural proximity of tryptic fragments provided information about the structural arrangement of the hydrophilic protein domains, which was integrated into a three-dimensional model of CopA. Comparative modeling of CopA was guided by the sequence similarity to the calcium ATPase of the sarcoplasmic reticulum, Serca1, for which detailed structures are available. In addition, known partial structures of CPx-ATPase homologous to CopA were used as modeling templates. A docking approach was used to predict the orientation of the heavy metal binding domain of CopA relative to the core structure, which was verified by distance constraints derived from cross-links. The overall structural model of CopA resembles the Serca1 structure, but reveals distinctive features of CPx-type ATPases. A prominent feature is the positioning of the heavy metal binding domain. It features an orientation of the Cu binding ligands which is appropriate for the interaction with Cu-loaded metallochaperones in solution. Moreover, a novel model of the architecture of the intramembranous Cu binding sites could be derived.

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“…GDP plays a role in the so-called G-protein systems [27] which utilize guanosine 5'-triphosphate (GTP 4À ) [28] and where metal ions are involved in the hydrolysis reactions [29] [30]. Cu 2 was selected because of its high affinity toward the N of guanosine in aqueous solution [18] [23] [31] and also because of its role in biology [32] [33].…”

Section: àmentioning

confidence: 99%

Influence of Decreasing Solvent Polarity (1,4‐Dioxane/Water Mixtures) on the Acid–Base and Copper(II)‐Binding Properties of Guanosine 5′‐Diphosphate

Bianchi

Griesser

Sigel

2005

Helvetica Chimica Acta

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Dedicated to Professor Dr. AndreÂ E. Merbach, on the occasion of his 65 th birthday, with admiration for his seminal contributions to chemistry and all best wishes for his future endeavors À is located mainly at the N(7) site and the other one at the terminal bphosphate group. In contrast, for 50% 1,4-dioxane/H 2 O solutions, a micro acidity-constant evaluation evidenced that ca. 75% of the H 2 (GDP)À species have both protons phosphate-bound, because the basicity of pyridinetype N sites decreases with decreasing solvent polarity whereas the one of phosphate groups increases. In the [Cu(H;GDP)] complex, the proton and the metal ion are in all three solvents overwhelmingly phosphatebound, and the release of this proton is inhibited by decreasing polarity of the solvent. Based on previously determined straight-line plots of log K À complex is more stable than expected based on the basicity of the diphosphate residue. This increased stability is attributed to macrochelate formation of the phosphate-coordinated Cu 2 with N(7) of the guanine residue. The formation degree of this macrochelate amounts in aqueous solution to ca. 75% (being thus higher than that of the Cu 2 complex of adenosine 5'-diphosphate) and in 50% (v/v) 1,4-dioxane/H 2 O to ca. 60%, i.e., the formation degree of the macrochelate is only relatively little affected by the change in solvent, though it needs to be emphasized that the overall stability of the [Cu(GDP)]À complex increases with decreasing solvent polarity. By including previously studied systems in the considerations, the biological implications are shortly discussed, and it is concluded that Nature has here a tool to alter the structure of complexes by shifting them on a protein surface from a polar to an apolar region and vice versa.

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Insights into the mechanism of copper transport by the Wilson and Menkes disease copper-transporting ATPases

Cited by 26 publications

References 77 publications

Structural Basis for the Function of the N-terminal Domain of the ATPase CopA from Bacillus subtilis

Structural Basis for the Function of the N-terminal Domain of the ATPase CopA from Bacillus subtilis

Structural model of the CopA copper ATPase of Enterococcus hirae based on chemical cross-linking

Influence of Decreasing Solvent Polarity (1,4‐Dioxane/Water Mixtures) on the Acid–Base and Copper(II)‐Binding Properties of Guanosine 5′‐Diphosphate

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