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- W3013668604 abstract "Abstract SERCA2b is a Ca 2+ -ATPase that pumps Ca 2+ from the cytosol into the ER and maintains the cellular calcium homeostasis. Herein, we present cryo-EM structures of human SERCA2b in E1·2Ca 2+ -AMPPCP and E2-BeF 3 - states at 2.9 and 2.8 Å resolutions, respectively. The structures revealed that the luminal extension tail (LE) characteristic of SERCA2b runs parallel to the lipid-water boundary near the luminal ends of transmembrane (TM) helices TM10 and TM7, and approaches the luminal loop flanked by TM7 and TM8. Upon deletion of the LE, the cytosolic- and TM-domain arrangement of SERCA2b resembled that of SERCA1a, resulting in multiple conformations. The LE regulates the conformational transition between the E1·2Ca 2+ -ATP and E2P states, explaining the different kinetic properties of SERCA2b from other isoforms lacking the LE. One sentence summary Cryo-EM structures of SERCA2b at 2.8-2.9 Å resolutions reveal how the luminal extension tail regulates its activity." @default.
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- W3013668604 date "2020-03-29" @default.
- W3013668604 modified "2023-10-16" @default.
- W3013668604 title "Cryo-EM structures of SERCA2b reveal the mechanism of regulation by the luminal extension tail" @default.
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- W3013668604 doi "https://doi.org/10.1101/2020.03.28.012849" @default.
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