2021 Fiscal Year Annual Research Report
New mechanisms of action of human calcium ATPase SERCA2b revealed by cryo-EM analysis
| Project/Area Number |
21K15036
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| Research Institution | Tohoku University |
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Principal Investigator |
張 玉霞 東北大学, 多元物質科学研究所, 助教 (10899769)
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| Project Period (FY) |
2021-04-01 – 2022-03-31
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| Keywords | cryo-EM / SERCA2b / Calcium pump |
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| Outline of Annual Research Achievements |
We newly determined several cryo-EM structures of SERCA2b, including a high-energy E1P state with two bound Ca ions and the post-E1P state immediately after Ca release. The dataset in E2P state identified a new conformation that differs from the conventional E2P state and the subsequent E2-Pi state that can be regarded as a late-stage Ca-unbound intermediate. The cryo-EM structures suggested that SERCA2b adopts multiple conformations in reaction and generates preformed states closely resembling the next intermediate. These findings provide essential structural insight into how enzymes work; multiple sub-states, including one highly similar to a next intermediate, are formed in a reaction intermediate to facilitate the transition step and thereby drive the catalytic cycle efficiently.
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