Copper binding triggers compaction in N-terminal tail of human copper pump ATP7B

Biochemical and Biophysical Research Communications
Tanumoy MondolPernilla Wittung-Stafshede

Abstract

Protein conformational changes are fundamental to biological reactions. For copper ion transport, the multi-domain protein ATP7B in the Golgi network receives copper from the cytoplasmic copper chaperone Atox1 and, with energy from ATP hydrolysis, moves the metal to the lumen for loading of copper-dependent enzymes. Although anticipated, conformational changes involved in ATP7B's functional cycle remain elusive. Using spectroscopic methods we here demonstrate that the four most N-terminal metal-binding domains in ATP7B, upon stoichiometric copper addition, adopt a more compact arrangement which has a higher thermal stability than in the absence of copper. In contrast to previous reports, no stable complex was found in solution between the metal-binding domains and the nucleotide-binding domain of ATP7B. Metal-dependent movement of the first four metal-binding domains in ATP7B may be a trigger that initiates the overall catalytic cycle.

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Citations

Oct 17, 2016·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Ranjeet KumarPernilla Wittung-Stafshede
Jun 28, 2017·Metallomics : Integrated Biometal Science·Kumaravel Ponnandai ShanmugavelPernilla Wittung-Stafshede
Oct 25, 2017·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Candan AriözPernilla Wittung-Stafshede
Jul 20, 2019·Metallomics : Integrated Biometal Science·Kumaravel Ponnandai Shanmugavel, Pernilla Wittung-Stafshede
Jan 1, 2018·Quarterly Reviews of Biophysics·Candan Ariöz, Pernilla Wittung-Stafshede
Oct 11, 2019·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Kumaravel Ponnandai ShanmugavelPernilla Wittung-Stafshede
Jul 30, 2019·International Journal of Biological Macromolecules·Giovanni GalloGabriella Fiorentino

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