Aarhus Universitets segl

Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

  • Ryuta Kanai
  • ,
  • Haruo Ogawa
  • ,
  • Bente Vilsen
  • Flemming Cornelius, Danmark
  • Chikashi Toyoshima
Na(+),K(+)-ATPase pumps three Na(+) ions out of cells in exchange for two K(+) taken up from the extracellular medium per ATP molecule hydrolysed, thereby establishing Na(+) and K(+) gradients across the membrane in all animal cells. These ion gradients are used in many fundamental processes, notably excitation of nerve cells. Here we describe 2.8 Å-resolution crystal structures of this ATPase from pig kidney with bound Na(+), ADP and aluminium fluoride, a stable phosphate analogue, with and without oligomycin that promotes Na(+) occlusion. These crystal structures represent a transition state preceding the phosphorylated intermediate (E1P) in which three Na(+) ions are occluded. Details of the Na(+)-binding sites show how this ATPase functions as a Na(+)-specific pump, rejecting K(+) and Ca(2+), even though its affinity for Na(+) is low (millimolar dissociation constant). A mechanism for sequential, cooperative Na(+) binding can now be formulated in atomic detail.
Sider (fra-til)201-6
Antal sider6
StatusUdgivet - 10 okt. 2013

Bibliografisk note

impact factor 38.6 (ISI Web of Knowledge)


  • Na bindingssteder

Se relationer på Aarhus Universitet Citationsformater

ID: 60633638