Crystal Structure of Na + , K + -ATPase in the Na + -Bound State-Reference-Cited by-同舟云学术

Crystal Structure of Na + , K + -ATPase in the Na + -Bound State

Published:2013-10-04 Issue:6154 Volume:342 Page:123-127
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Nyblom Maria¹²,Poulsen Hanne¹²³,Gourdon Pontus¹²³,Reinhard Linda¹²,Andersson Magnus⁴,Lindahl Erik⁴⁵,Fedosova Natalya¹⁶,Nissen Poul¹²³

Affiliation:

1. Centre for Membrane Pumps in Cells and Disease–PUMPkin, Danish National Research Foundation, DK-8000 Aarhus, Denmark.

2. Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10c, DK-8000 Aarhus, Denmark.

3. Danish Research Institute for Translational Neuroscience-DANDRITE, Nordic-EMBL Partnership of Molecular Medicine, Aarhus, Denmark.

4. Science for Life Laboratory, Theoretical and Computational Biophysics, Department of Theoretical Physics, Swedish e-Science Research Center, KTH Royal Institute of Technology, SE-171 21 Solna, Sweden.

5. Science for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.

6. Department of Biomedicine, Aarhus University, Ole Worms Allé 4, Building 1182, DK-8000 Aarhus, Denmark.

Abstract

Pumping Out Sodium Mammalian cells contain relatively high concentrations of potassium but low concentrations of sodium. This balance is maintained by an ion pump, the Na + , K + –adenosine triphosphatase, in an adenosine triphosphate–driven transport cycle that results in the export of three sodium ions and the import of two potassium ions. Structures of potassium-bound conformations of the pump have been determined. Now, Nyblom et al. (p. 123 , published online 19 September) report on the high-resolution crystal structure of a Na + -bound conformation, which reveals conformational changes associated with Na + binding.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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