ATP-synthesis in archaea: Structure-function relations of the halobacterial A-ATPase

Abstract

The archaeal (A)-ATPase has been described as a chimeric energy converter with close relationship to both the vacuolar ATPase class in higher eukaryotes and the coupling factor (F)-ATPase class in eubacteria, mitochondria and chloroplasts. With respect to their structure and some inhibitor responses, A-ATPases are more closely related to the vacuolar ATPase type than to F-ATPase. Their function, ATP synthesis at the expense of an ion gradient, however, is a typical attribute of the F-ATPase class. V-type ATPases serve as generators of a proton gradient driving the accumulation of solutes within vesicles such as the vacuoles of plant cells. The three catalytic subunits (A) of the archaeal ATPases are the largest subunits of the A1-part and, like in V-ATPases, closer related to the F-ATPase β-subunits, whereas B corresponds to F-ATPase α. The catalytic subunits A of archaeal ATPases contain an insert of about 80 amino acids in their primary structures that may be aligned to comparable structures in V-ATPases. The location of this additional peptide in Haloferax volcanii is shown using the 2.8 A X-ray resolution of the bovine mitochondrial F-ATPase [Abrahams et al. (1994) Nature 370: 621-628]. A three dimensional structure for the catalytic subunit of Haloferax volcanii ATPase is proposed using the Swiss-Model Automated Protein Modelling Server. The halobacterial ATPase is a halophilic protein; it contains about 20% negatively charged amino acid residues. A large portion of acidic residues is located on the outer surface of the protein as well as in the insert of subunit A. This result is discussed in terms of protein stability under high salt stress conditions.