Mechanical inhibition of isolated Vo from V/A-ATPase for proton conductance
V-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V1 domain, with proton flow through the Vo membrane domain, via rotation of the central rotor complex relative to the surrounding stator apparatus. Upon dissociation from the V1 domain, the Vo domain of the...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2020-07-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/56862 |
| _version_ | 1828376056531255296 |
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| author | Jun-ichi Kishikawa Atsuko Nakanishi Aya Furuta Takayuki Kato Keiichi Namba Masatada Tamakoshi Kaoru Mitsuoka Ken Yokoyama |
| author_facet | Jun-ichi Kishikawa Atsuko Nakanishi Aya Furuta Takayuki Kato Keiichi Namba Masatada Tamakoshi Kaoru Mitsuoka Ken Yokoyama |
| author_sort | Jun-ichi Kishikawa |
| collection | DOAJ |
| description | V-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V1 domain, with proton flow through the Vo membrane domain, via rotation of the central rotor complex relative to the surrounding stator apparatus. Upon dissociation from the V1 domain, the Vo domain of the eukaryotic V-ATPase can adopt a physiologically relevant auto-inhibited form in which proton conductance through the Vo domain is prevented, however the molecular mechanism of this inhibition is not fully understood. Using cryo-electron microscopy, we determined the structure of both the holo V/A-ATPase and isolated Vo at near-atomic resolution, respectively. These structures clarify how the isolated Vo domain adopts the auto-inhibited form and how the holo complex prevents formation of the inhibited Vo form. |
| first_indexed | 2024-04-14T07:53:58Z |
| format | Article |
| id | doaj.art-9b8c79b57c2a4057b6a108a7260c05dc |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-14T07:53:58Z |
| publishDate | 2020-07-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-9b8c79b57c2a4057b6a108a7260c05dc2022-12-22T02:05:06ZengeLife Sciences Publications LtdeLife2050-084X2020-07-01910.7554/eLife.56862Mechanical inhibition of isolated Vo from V/A-ATPase for proton conductanceJun-ichi Kishikawa0https://orcid.org/0000-0003-3913-7330Atsuko Nakanishi1Aya Furuta2Takayuki Kato3Keiichi Namba4Masatada Tamakoshi5Kaoru Mitsuoka6Ken Yokoyama7https://orcid.org/0000-0002-6813-1096Department of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto, Japan; Institute for Protein Research, Osaka University, Suita, JapanDepartment of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto, Japan; Research Center for Ultra-High Voltage Electron Microscopy, Osaka University, Research Center for Ultra-High Voltage Electron Microscopy, Mihogaoka, Osaka, JapanDepartment of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto, JapanInstitute for Protein Research, Osaka University, Suita, Japan; Graduate School of Frontier Biosciences, Osaka University, Suita, JapanGraduate School of Frontier Biosciences, Osaka University, Suita, Japan; RIKEN Center for Biosystems Dynamics Research and SPring-8 Center, Suita, Japan; JEOL YOKOGUSHI Research Alliance Laboratories, Osaka University, Suita, JapanDepartment of Molecular Biology, Tokyo University of Pharmacy and Life Sciences, Horinouchi, Hachioji, Tokyo, JapanResearch Center for Ultra-High Voltage Electron Microscopy, Osaka University, Research Center for Ultra-High Voltage Electron Microscopy, Mihogaoka, Osaka, JapanDepartment of Molecular Biosciences, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto, JapanV-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V1 domain, with proton flow through the Vo membrane domain, via rotation of the central rotor complex relative to the surrounding stator apparatus. Upon dissociation from the V1 domain, the Vo domain of the eukaryotic V-ATPase can adopt a physiologically relevant auto-inhibited form in which proton conductance through the Vo domain is prevented, however the molecular mechanism of this inhibition is not fully understood. Using cryo-electron microscopy, we determined the structure of both the holo V/A-ATPase and isolated Vo at near-atomic resolution, respectively. These structures clarify how the isolated Vo domain adopts the auto-inhibited form and how the holo complex prevents formation of the inhibited Vo form.https://elifesciences.org/articles/56862single particle cryo-emrotary ATPaseV/A-ATPaseATP synthase |
| spellingShingle | Jun-ichi Kishikawa Atsuko Nakanishi Aya Furuta Takayuki Kato Keiichi Namba Masatada Tamakoshi Kaoru Mitsuoka Ken Yokoyama Mechanical inhibition of isolated Vo from V/A-ATPase for proton conductance eLife single particle cryo-em rotary ATPase V/A-ATPase ATP synthase |
| title | Mechanical inhibition of isolated Vo from V/A-ATPase for proton conductance |
| title_full | Mechanical inhibition of isolated Vo from V/A-ATPase for proton conductance |
| title_fullStr | Mechanical inhibition of isolated Vo from V/A-ATPase for proton conductance |
| title_full_unstemmed | Mechanical inhibition of isolated Vo from V/A-ATPase for proton conductance |
| title_short | Mechanical inhibition of isolated Vo from V/A-ATPase for proton conductance |
| title_sort | mechanical inhibition of isolated vo from v a atpase for proton conductance |
| topic | single particle cryo-em rotary ATPase V/A-ATPase ATP synthase |
| url | https://elifesciences.org/articles/56862 |
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