F-type or V-type? The chimeric nature of the archaebacterial ATP synthase

Biochim Biophys Acta. 1992 Jul 17;1101(2):232-5. doi: 10.1016/0005-2728(92)90233-r.


Archaebacterial plasma membranes contain an ATPase acting in vivo as a delta mu H(+)-driven ATP synthase. While functional features and their general structural design are resembling F-type ATPases, primary sequences of the two large polypeptides from the catalytic part are closely related to V-type ATPases from eucaryotic vacuolar membranes. The chimeric nature of archaebacterial ATPase from Sulfolobus was investigated in terms of nucleotide interactions and related to specific sequence parameters in a comparison to well known F- and V-type ATPases. The study disclosed a general difference of F- and V-type ATPases at one class of the nucleotide binding sites.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Archaea / enzymology*
  • Binding Sites
  • Chimera
  • Molecular Sequence Data
  • Protein Conformation
  • Proton-Translocating ATPases / chemistry*
  • Proton-Translocating ATPases / metabolism
  • Sequence Alignment


  • Proton-Translocating ATPases

Associated data