Rotation,Structure, and Classification of Prokaryotic V-ATPase |
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Authors: | Email author" target="_blank">Ken?YokoyamaEmail author Hiromi?Imamura |
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Institution: | (1) ATP System Project, Exploratory Research for Advanced Technology, Japan Science and Technology Agency, Nagatsuta, Midori-ku, Yokohama, Japan;(2) ATP System Project, Exploratory Research for Advanced Technology, Japan Science and Technology Agency, 5800-3 Nagatsuta, Midori-ku Yokohama, 226-0026, Japan |
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Abstract: | 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 V0 domain in order to accommodate the V1 central stalk. This structure seems essential for the regulatory reversible association/dissociation of the V1 and the V0 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). |
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Keywords: | V-ATPase ATP synthase single-molecule X-ray crystallography Thermus thermophilus |
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