Rotation, structure, and classification of prokaryotic V-ATPase.
The prokaryotic V-type ATPase/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/function relationships in the V-ATPase from the eubacterium Thermus thermophilus. First, we describe single-molecule analyses of T. thermophilus V-ATPase. Using the single-molecule technique, it was established that the V-ATPase is a rotary motor. Second, we discuss arrangement of subunits in V-ATPase. Third, the crystal structure of the C-subunit (homolog of eukaryotic d-subunit) is described. This funnel-shape subunit appears to cap the proteolipid ring in the V(0) domain in order to accommodate the V(1) central stalk. This structure seems essential for the regulatory reversible association/dissociation of the V(1) and the V(0) domains. Last, we discuss classification of the V-ATPase family. We propose that the term prokaryotic V-ATPases should be used rather than the term archaeal-type ATPase (A-ATPase).
Yokoyama
Ken
K
ATP System Project, Exploratory Research for Advanced Technology, Japan Science and Technology Agency, Nagatsuta, Midori-ku, Yokohama, Japan. kyokoyama-ra@res.titech.ac.jp
Imamura
Hiromi
H
D018360:Crystallography, X-Ray; D020409:Molecular Motor Proteins; D011387:Prokaryotic Cells; D020836:Protein Structure, Quaternary; D016963:Thermus thermophilus / Q000201:enzymology*; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry* / Q000145:classification
D020409:Molecular Motor Proteins; D025262:Vacuolar Proton-Translocating ATPases