Rotation, Structure, and Classification of Prokaryotic V-ATPase

• Published in: Journal of bioenergetics and biomembranes Vol. 37; no. 6; pp. 405 - 410
• Main Authors: Yokoyama, Ken, Imamura, Hiromi
• Format: Journal Article
• Language: English
• Published: United States Springer Nature B.V 01.12.2005
• Subjects: Adenosine triphosphatase; Bacteria; Classification; Crystal structure; Crystallography, X-Ray; Domains; Enzymes; H+-transporting ATPase; Homology; Molecular Motor Proteins; Prokaryotic Cells; Protein Structure, Quaternary; Structure-function relationships; Thermus thermophilus - enzymology; Vacuolar Proton-Translocating ATPases - chemistry; Vacuolar Proton-Translocating ATPases - classification
• ISSN: 0145-479X; 1573-6881
• DOI: 10.1007/s10863-005-9480-1

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).