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Copper binding triggers compaction in N-terminal tail of human copper pump ATP7B
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Biology and Biological Engineering Department, Chalmers University of Technology, Gothenburg, Sweden.
2016 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 470, no 3, 663-669 p.Article in journal (Refereed) PublishedText
Abstract [en]

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.

Place, publisher, year, edition, pages
Elsevier, 2016. Vol. 470, no 3, 663-669 p.
Keyword [en]
Protein-protein interactions, Metalloenzymes, Copper transport, NMR, Circular dichroism, Conformational changes
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
URN: urn:nbn:se:umu:diva-118252DOI: 10.1016/j.bbrc.2016.01.085ISI: 000370467100030PubMedID: 26797276OAI: oai:DiVA.org:umu-118252DiVA: diva2:912765
Available from: 2016-03-17 Created: 2016-03-14 Last updated: 2016-03-17Bibliographically approved

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Mondol, TanumoyÅdén, JörgenWittung-Stafshede, Pernilla
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Biochemical and Biophysical Research Communications - BBRC
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

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