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  • Title: F-type or V-type? The chimeric nature of the archaebacterial ATP synthase.
    Author: Schäfer G, Meyering-Vos M.
    Journal: Biochim Biophys Acta; 1992 Jul 17; 1101(2):232-5. PubMed ID: 1385979.
    Abstract:
    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.
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