Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Atx1 | the metallo-chaperone Atx1 interacts with the N-terminus of Ccc2 essentially required for the copper delivery to the trans-Golgi network. Atx1 does not activate the Ccc2-derived ATPase lacking its N-terminus | Saccharomyces cerevisiae |
Cloned (Comment) | Organism |
---|---|
co-expression of Atx1 and Ccc2 mutants in an atx1Dccc2D yeast strain | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of the DELTAMBDCcc2 mutant lacking the N-terminus. In vivo Atx1-M1 or Atx1-M2 interactions activate Ccc2, however, M1 or M2, expressed in place of the metallo-chaperone Atx1, are not as efficient as Atx1 in delivering copper to the Ccc2 N-terminus. But when the Ccc2 N-terminus is truncated in mutant DELTAMBDCcc2, these independent metal-binding domains behave like functional metallo-chaperones in delivering copper to another copper-binding site in Ccc2. Both M1 and M2, when expressed as independent cytosolic proteins, are able to bind copper in the cytosol and transfer this metal to a copper-binding site in Ccc2, out of the N-terminus | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
Golgi membrane | of the trans-Golgi network | Saccharomyces cerevisiae | 139 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + Cu2+/in | Saccharomyces cerevisiae | the Ccc2 N-terminus encloses two copper-binding domains, M1 and M2, in vivo Atx1-M1 or Atx1-M2 interactions activate Ccc2. Dual role for the Ccc2 N-terminus, namely to receive copper from Atx1 and to convey copper to another domain of Ccc2, overview | ADP + phosphate + Cu2+/out | - |
? | |
ATP + H2O + Cu2+/in | Saccharomyces cerevisiae BY4741 | the Ccc2 N-terminus encloses two copper-binding domains, M1 and M2, in vivo Atx1-M1 or Atx1-M2 interactions activate Ccc2. Dual role for the Ccc2 N-terminus, namely to receive copper from Atx1 and to convey copper to another domain of Ccc2, overview | ADP + phosphate + Cu2+/out | - |
? | |
ATP + H2O + Cu2+/in | Saccharomyces cerevisiae YPH499 | the Ccc2 N-terminus encloses two copper-binding domains, M1 and M2, in vivo Atx1-M1 or Atx1-M2 interactions activate Ccc2. Dual role for the Ccc2 N-terminus, namely to receive copper from Atx1 and to convey copper to another domain of Ccc2, overview | ADP + phosphate + Cu2+/out | - |
? | |
additional information | Saccharomyces cerevisiae | enzymatic cycle of Ccc2: the ATPase binds Cu(I) at its transport site, a step which induces a conformational change and phosphorylation from ATP. The energy is used to open the transport site on the other side of the membrane and to release Cu(I) into the TGN lumen, the aspartyl-phosphate bound is hydrolyzed | ? | - |
? | |
additional information | Saccharomyces cerevisiae BY4741 | enzymatic cycle of Ccc2: the ATPase binds Cu(I) at its transport site, a step which induces a conformational change and phosphorylation from ATP. The energy is used to open the transport site on the other side of the membrane and to release Cu(I) into the TGN lumen, the aspartyl-phosphate bound is hydrolyzed | ? | - |
? | |
additional information | Saccharomyces cerevisiae YPH499 | enzymatic cycle of Ccc2: the ATPase binds Cu(I) at its transport site, a step which induces a conformational change and phosphorylation from ATP. The energy is used to open the transport site on the other side of the membrane and to release Cu(I) into the TGN lumen, the aspartyl-phosphate bound is hydrolyzed | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Saccharomyces cerevisiae BY4741 | - |
- |
- |
Saccharomyces cerevisiae YPH499 | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + Cu2+/in | the Ccc2 N-terminus encloses two copper-binding domains, M1 and M2, in vivo Atx1-M1 or Atx1-M2 interactions activate Ccc2. Dual role for the Ccc2 N-terminus, namely to receive copper from Atx1 and to convey copper to another domain of Ccc2, overview | Saccharomyces cerevisiae | ADP + phosphate + Cu2+/out | - |
? | |
ATP + H2O + Cu2+/in | the Ccc2 N-terminus encloses two copper-binding domains, M1 and M2, in vivo Atx1-M1 or Atx1-M2 interactions activate Ccc2. Dual role for the Ccc2 N-terminus, namely to receive copper from Atx1 and to convey copper to another domain of Ccc2, overview | Saccharomyces cerevisiae BY4741 | ADP + phosphate + Cu2+/out | - |
? | |
ATP + H2O + Cu2+/in | the Ccc2 N-terminus encloses two copper-binding domains, M1 and M2, in vivo Atx1-M1 or Atx1-M2 interactions activate Ccc2. Dual role for the Ccc2 N-terminus, namely to receive copper from Atx1 and to convey copper to another domain of Ccc2, overview | Saccharomyces cerevisiae YPH499 | ADP + phosphate + Cu2+/out | - |
? | |
additional information | enzymatic cycle of Ccc2: the ATPase binds Cu(I) at its transport site, a step which induces a conformational change and phosphorylation from ATP. The energy is used to open the transport site on the other side of the membrane and to release Cu(I) into the TGN lumen, the aspartyl-phosphate bound is hydrolyzed | Saccharomyces cerevisiae | ? | - |
? | |
additional information | enzymatic cycle of Ccc2: the ATPase binds Cu(I) at its transport site, a step which induces a conformational change and phosphorylation from ATP. The energy is used to open the transport site on the other side of the membrane and to release Cu(I) into the TGN lumen, the aspartyl-phosphate bound is hydrolyzed | Saccharomyces cerevisiae BY4741 | ? | - |
? | |
additional information | enzymatic cycle of Ccc2: the ATPase binds Cu(I) at its transport site, a step which induces a conformational change and phosphorylation from ATP. The energy is used to open the transport site on the other side of the membrane and to release Cu(I) into the TGN lumen, the aspartyl-phosphate bound is hydrolyzed | Saccharomyces cerevisiae YPH499 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Ccc2 | - |
Saccharomyces cerevisiae |
copper ATPase | - |
Saccharomyces cerevisiae |
More | the enzyme belongs to the P-type ATPases | Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
metabolism | copper delivery to the secretory pathway in yeast, and enzymatic cycle of Ccc2, modelling, overview | Saccharomyces cerevisiae |
physiological function | copper delivery to the trans-Golgi network involves interactions between the metallo-chaperone Atx1 and the N-terminus of Ccc2, the P-type ATPase responsible for copper transport across trans-Golgi network membranes. Disruption of the Atx1-Ccc2 route leads to cell growth arrest in a copper-and-iron-limited medium, Atx1-Ccc2 and intra-Ccc2 domain-domain interactions, overview | Saccharomyces cerevisiae |