ABSTRACT
The eukaryotic V-ATPases function as proton pumps that are
involved in the acidification of cellular compartments such as the
Golgi apparatus or lysosomes. In addition, some prokaryotes, such as
the Thermus thermophilus or Enterococcus hirae, contain a member of the family (or homologue) of the V-ATPases in their membranes.
The prokaryotic V-type ATPases/synthases (prokaryotic V-ATPases)
have simpler subunit compositions than eukaryotic V-ATPases
and, thus, are useful subjects for studying chemical, physical, and
structural properties of V-ATPase. In this review, we focus on the
results of recent studies on the structure of the V-ATPase from the
eubacteria, both T. thermophilus and E. hirae.