Crystal structure of subunits D and F in complex gives insight into energy transmission of the eukaryotic V-ATPase from Saccharomyces cerevisiae

• المؤلفون الرئيسيون: Balakrishna, Asha Manikkoth, Basak, Sandip, Manimekalai, Malathy Sony Subramanian, Grüber, Gerhard
• مؤلفون آخرون: School of Biological Sciences
• التنسيق: مقال
• اللغة: English
• منشور في: 2018
• الموضوعات: Bioenergetics; ATP Synthase; DRNTU::Science::Biological sciences
• الوصول للمادة أونلاين: https://hdl.handle.net/10356/88974; http://hdl.handle.net/10220/46056
• المؤسسة: Nanyang Technological University

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...