Crystal structure of subunits D and F in complex gives insight into energy transmission of the eukaryotic V-ATPase from Saccharomyces cerevisiae
Eukaryotic V1VO-ATPases hydrolyze ATP in the V1 domain coupled to ion pumping in VO. A unique mode of regulation of V-ATPases is the reversible disassembly of V1 and VO, which reduces ATPase activity and causes silencing of ion conduction. The subunits D and F are proposed to be key in these enzymat...
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Main Authors: | , , , |
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格式: | Article |
語言: | English |
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2018
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在線閱讀: | https://hdl.handle.net/10356/88974 http://hdl.handle.net/10220/46056 |
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機構: | Nanyang Technological University |
語言: | English |