7W7V

'late' E2P of SERCA2b

Summary for 7W7V

• Entry DOI: 10.2210/pdb7w7v/pdb
• EMDB information: 32349
• Descriptor: Sarcoplasmic/endoplasmic reticulum calcium ATPase 2, BERYLLIUM TRIFLUORIDE ION, MAGNESIUM ION (3 entities in total)
• Functional Keywords: calcium, metal transport
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 114959.98

Authors

Zhang, Y.,Watanabe, S.,Tsutsumi, A.,Inaba, K. (deposition date: 2021-12-06, release date: 2022-12-14, Last modification date: 2024-06-26)

Primary citation

Zhang, Y.,Kobayashi, C.,Cai, X.,Watanabe, S.,Tsutsumi, A.,Kikkawa, M.,Sugita, Y.,Inaba, K.
Multiple sub-state structures of SERCA2b reveal conformational overlap at transition steps during the catalytic cycle.
Cell Rep, 41:111760-111760, 2022

PubMed Abstract: Sarco/endoplasmic reticulum Ca ATPase (SERCA) pumps Ca into the endoplasmic reticulum (ER). Herein, we present cryo-electron microscopy (EM) structures of three intermediates of SERCA2b: Ca-bound phosphorylated (E1P·2Ca) and Ca-unbound dephosphorylated (E2·Pi) intermediates and another between the E2P and E2·Pi states. Our cryo-EM analysis demonstrates that the E1P·2Ca state exists in low abundance and preferentially transitions to an E2P-like structure by releasing Ca and that the Ca 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.

PubMed: 36476867
DOI: 10.1016/j.celrep.2022.111760

Experimental method

ELECTRON MICROSCOPY (3 Å)