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Multiple sub-state structures of SERCA2b reveal conformational overlap at transition steps during the catalytic cycle by Yuxia Zhang; Chigusa Kobayashi; Xiaohan Cai; Satoshi Watanabe; Akihisa Tsutsumi; Masahide Kikkawa; Yuji Sugita; Kenji Inaba is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Multiple sub-state structures of SERCA2b reveal conformational overlap at transition steps during the catalytic cycle about?

Sarco/endoplasmic reticulum Ca 2+ ATPase (SERCA) pumps Ca 2+ into the endoplasmic reticulum (ER). Herein, we present cryo-electron microscopy (EM) structures of three intermediates of SERCA2b: Ca 2+ -bound phosphorylated (E1P$2Ca 2+ ) and Ca 2+ -unbound dephosphorylated (E2$Pi) intermediates and another between the E2P and E2$Pi states. Our cryo-EM analysis demonstrates that the E1P$2Ca 2+ state exists in low abundance and preferentially transitions to an E2P-like structure by releasing Ca 2+ and that the Ca 2+ release gate subsequently undergoes stepwise closure during the dephosphorylation processes. Importantly, each intermediate adopts multiple sub-state structures including those like the next one in the catalytic series, indicating conformational overlap at transition steps, as further substantiated by atomistic molecular dynamic simulations of SERCA2b in a lipid bilayer. The present findings provide insight into how enzymes accelerate catalytic cycles.

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Author

Yuxia Zhang; Chigusa Kobayashi; Xiaohan Cai; Satoshi Watanabe; Akihisa Tsutsumi; Masahide Kikkawa; Yuji Sugita; Kenji Inaba

Publisher

Elsevier BV

Published

2022

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)