期刊
FEBS JOURNAL
卷 278, 期 17, 页码 3025-3031出版社
WILEY
DOI: 10.1111/j.1742-4658.2011.08222.x
关键词
atomic force microscopy; ion pump; P-type ATPase; SERCA; single molecular reaction analysis
资金
- SENTAN
- JST
- Ministry of Education, Culture, Sports, Science and Technology, Japan [20059018]
- Grants-in-Aid for Scientific Research [20059018, 22770148] Funding Source: KAKEN
Studies of ion pumps, such as ATP synthetase and Ca2+-ATPase, have a long history. The crystal structures of several kinds of ion pump have been resolved, and provide static pictures of mechanisms of ion transport. In this study, using fast-scanning atomic force microscopy, we have visualized conformational changes in the sarcoplasmic reticulum Ca2+-ATPase (SERCA) in real time at the single-molecule level. The analyses of individual SERCA molecules in the presence of both ATP and free Ca2+ revealed up-down structural changes corresponding to the Albers-Post scheme. This fluctuation was strongly affected by the ATP and Ca2+ concentrations, and was prevented by an inhibitor, thapsigargin. Interestingly, at a physiological ATP concentrations, the up-down motion disappeared completely. These results indicate that SERCA does not transit through the shortest structure, and has a catalytic pathway different from the ordinary Albers-Post scheme under physiological conditions.
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