Cryo-EM studies of the rotary H<sup>+</sup>-ATPase/synthase from <i>Thermus thermophilus</i>
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- Nakanishi Atsuko
- Department of Molecular Biosciences, Kyoto Sangyo University
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- Kishikawa Jun-ichi
- Department of Molecular Biosciences, Kyoto Sangyo University
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- Mitsuoka Kaoru
- Research Center for Ultra-High Voltage Electron Microscopy, Osaka University
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- Yokoyama Ken
- Department of Molecular Biosciences, Kyoto Sangyo University
Description
<p>Proton-translocating rotary ATPases couple proton influx across the membrane domain and ATP hydrolysis/synthesis in the soluble domain through rotation of the central rotor axis against the surrounding peripheral stator apparatus. It is a significant challenge to determine the structure of rotary ATPases due to their intrinsic conformational heterogeneity and instability. Recent progress of single particle analysis of protein complexes using cryogenic electron microscopy (cryo-EM) has enabled the determination of whole rotary ATPase structures and made it possible to classify different rotational states of the enzymes at a near atomic resolution. Three cryo-EM maps corresponding to different rotational states of the V/A type H+-rotary ATPase from a bacterium Thermus thermophilus provide insights into the rotation of the whole complex, which allow us to determine the movement of each subunit during rotation. In addition, this review describes methodological developments to determine higher resolution cryo-EM structures, such as specimen preparation, to improve the image contrast of membrane proteins.</p>
Journal
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- Biophysics and Physicobiology
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Biophysics and Physicobiology 16 (0), 140-146, 2019
The Biophysical Society of Japan
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Keywords
Details 詳細情報について
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- CRID
- 1390282752322324096
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- NII Article ID
- 130007701812
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- ISSN
- 21894779
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- Text Lang
- en
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- Data Source
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- JaLC
- Crossref
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed