New insights into structure-function relationships between archeal ATP synthase (A1A0) and vacuolar type ATPase (V1V0)

Bioessays. 2008 Nov;30(11-12):1096-109. doi: 10.1002/bies.20827.


Adenosine triphosphate, ATP, is the energy currency of living cells. While ATP synthases of archae and ATP synthases of pro- and eukaryotic organisms operate as energy producers by synthesizing ATP, the eukaryotic V-ATPase hydrolyzes ATP and thus functions as energy transducer. These enzymes share features like the hydrophilic catalytic- and the membrane-embedded ion-translocating sector, allowing them to operate as nano-motors and to transform the transmembrane electrochemical ion gradient into ATP or vice versa. Since archaea are rooted close to the origin of life, the A-ATP synthase is probably more similar in its composition and function to the "original" enzyme, invented by Nature billion years ago. On the contrary, the V-ATPases have acquired specific structural, functional and regulatory features during evolution. This review will summarize the current knowledge on the structure, mechanism and regulation of A-ATP synthases and V-ATPases. The importance of V-ATPase in pathophysiology of diseases will be discussed.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Triphosphate / chemistry
  • Archaea / metabolism*
  • Catalysis
  • Crystallography, X-Ray / methods
  • Electrochemistry / methods
  • Humans
  • Models, Biological
  • Models, Molecular
  • Molecular Conformation
  • Nanotechnology / methods
  • Nucleotides / chemistry
  • Protein Binding
  • Protein Conformation
  • Structure-Activity Relationship
  • Vacuolar Proton-Translocating ATPases / chemistry*
  • Vacuolar Proton-Translocating ATPases / physiology*


  • Nucleotides
  • Adenosine Triphosphate
  • Vacuolar Proton-Translocating ATPases