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EnglishSarco/endoplasmic reticulum Ca2+ ATPase (SERCA) transporters regulate calcium signaling by active calcium ion reuptake to internal stores. Structural transitions associated with transport have been characterized by x-ray crystallography, but critical intermediates involved in the accessibility switch across the membrane are missing. We combined time-resolved x-ray solution scattering (TR-XSS) experiments and molecular dynamics (MD) simulations for real-time tracking of concerted SERCA reaction cycle dynamics in the native membrane. The equilibrium [Ca2] E1 state before laser activation differed in the domain arrangement compared with crystal structures, and following laser-induced release of caged ATP, a 1.5-ms intermediate was formed that showed closure of the cytoplasmic domains typical of E1 states with bound Ca2+ and ATP. A subsequent 13-ms transient state showed a previously unresolved actuator (A) domain arrangement that exposed the ADP-binding site after phosphorylation. Hence, the obtained TR-XSS models determine the relative timing of so-far elusive domain rearrangements in a native environment.
Ravishankar H., Pedersen M.N., Eklund M., Sitsel A., Li C., Duelli A., et al. (2020). Tracking Ca2+ ATPase intermediates in real time by x-ray solution scattering. SCIENCE ADVANCES, 6(12), eaaz0981 [10.1126/sciadv.aaz0981].
| Data di pubblicazione: | 2020 | |
| Titolo: | Tracking Ca2+ ATPase intermediates in real time by x-ray solution scattering | |
| Autori: | ||
| Citazione: | Ravishankar H., Pedersen M.N., Eklund M., Sitsel A., Li C., Duelli A., et al. (2020). Tracking Ca2+ ATPase intermediates in real time by x-ray solution scattering. SCIENCE ADVANCES, 6(12), eaaz0981 [10.1126/sciadv.aaz0981]. | |
| Rivista: | ||
| Digital Object Identifier (DOI): | http://dx.doi.org/10.1126/sciadv.aaz0981 | |
| Abstract: | Sarco/endoplasmic reticulum Ca2+ ATPase (SERCA) transporters regulate calcium signaling by active calcium ion reuptake to internal stores. Structural transitions associated with transport have been characterized by x-ray crystallography, but critical intermediates involved in the accessibility switch across the membrane are missing. We combined time-resolved x-ray solution scattering (TR-XSS) experiments and molecular dynamics (MD) simulations for real-time tracking of concerted SERCA reaction cycle dynamics in the native membrane. The equilibrium [Ca2] E1 state before laser activation differed in the domain arrangement compared with crystal structures, and following laser-induced release of caged ATP, a 1.5-ms intermediate was formed that showed closure of the cytoplasmic domains typical of E1 states with bound Ca2+ and ATP. A subsequent 13-ms transient state showed a previously unresolved actuator (A) domain arrangement that exposed the ADP-binding site after phosphorylation. Hence, the obtained TR-XSS models determine the relative timing of so-far elusive domain rearrangements in a native environment. | |
| Settore Scientifico Disciplinare: | Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin) | |
| Appare nelle tipologie: | 1.01 Articolo in rivista |
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| eaaz0981.full.pdf | Versione Editoriale | Open Access Visualizza/Apri |
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