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Structure and Function of Cu(I)- and Zn(II)-ATPases.
Sitsel, Oleg; Grønberg, Christina; Autzen, Henriette Elisabeth; Wang, Kaituo; Meloni, Gabriele; Nissen, Poul; Gourdon, Pontus.
Afiliación
  • Sitsel O; Centre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Department of Molecular Biology and Genetics, Aarhus University , Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark.
  • Grønberg C; Department of Biomedical Sciences, University of Copenhagen , Blegdamsvej 3B, DK-2200 Copenhagen, Denmark.
  • Autzen HE; Department of Biomedical Sciences, University of Copenhagen , Blegdamsvej 3B, DK-2200 Copenhagen, Denmark.
  • Wang K; Department of Biomedical Sciences, University of Copenhagen , Blegdamsvej 3B, DK-2200 Copenhagen, Denmark.
  • Meloni G; Division of Chemistry and Chemical Engineering and Howard Hughes Medical Institute, California Institute of Technology , Pasadena, California 91125, United States.
  • Nissen P; Centre for Membrane Pumps in Cells and Disease (PUMPkin), Danish National Research Foundation, Department of Molecular Biology and Genetics, Aarhus University , Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark.
  • Gourdon P; Department of Biomedical Sciences, University of Copenhagen , Blegdamsvej 3B, DK-2200 Copenhagen, Denmark.
Biochemistry ; 54(37): 5673-83, 2015 Sep 22.
Article en En | MEDLINE | ID: mdl-26132333
Copper and zinc are micronutrients essential for the function of many enzymes while also being toxic at elevated concentrations. Cu(I)- and Zn(II)-transporting P-type ATPases of subclass 1B are of key importance for the homeostasis of these transition metals, allowing ion transport across cellular membranes at the expense of ATP. Recent biochemical studies and crystal structures have significantly improved our understanding of the transport mechanisms of these proteins, but many details about their structure and function remain elusive. Here we compare the Cu(I)- and Zn(II)-ATPases, scrutinizing the molecular differences that allow transport of these two distinct metal types, and discuss possible future directions of research in the field.
Asunto(s)

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Zinc / Adenosina Trifosfatasas / Cobre / Proteínas de Transporte de Catión Idioma: En Revista: Biochemistry Año: 2015 Tipo del documento: Article País de afiliación: Dinamarca

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Zinc / Adenosina Trifosfatasas / Cobre / Proteínas de Transporte de Catión Idioma: En Revista: Biochemistry Año: 2015 Tipo del documento: Article País de afiliación: Dinamarca