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Tracking Ca2+ ATPase intermediates in real time by x-ray solution scattering

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Tracking Ca2+ ATPase intermediates in real time by x-ray solution scattering. / Ravishankar, Harsha; Pedersen, Martin Nors; Eklund, Mattias et al.

I: Science Advances, Bind 6, Nr. 12, eaaz0981, 03.2020.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Harvard

Ravishankar, H, Pedersen, MN, Eklund, M, Sitsel, A, Li, C, Duelli, A, Levantino, M, Wulff, M, Barth, A, Olesen, C, Nissen, P & Andersson, M 2020, 'Tracking Ca2+ ATPase intermediates in real time by x-ray solution scattering', Science Advances, bind 6, nr. 12, eaaz0981. https://doi.org/10.1126/sciadv.aaz0981

APA

Ravishankar, H., Pedersen, M. N., Eklund, M., Sitsel, A., Li, C., Duelli, A., Levantino, M., Wulff, M., Barth, A., Olesen, C., Nissen, P., & Andersson, M. (2020). Tracking Ca2+ ATPase intermediates in real time by x-ray solution scattering. Science Advances, 6(12), [eaaz0981]. https://doi.org/10.1126/sciadv.aaz0981

CBE

Ravishankar H, Pedersen MN, Eklund M, Sitsel A, Li C, Duelli A, Levantino M, Wulff M, Barth A, Olesen C, et al. 2020. Tracking Ca2+ ATPase intermediates in real time by x-ray solution scattering. Science Advances. 6(12):Article eaaz0981. https://doi.org/10.1126/sciadv.aaz0981

MLA

Ravishankar, Harsha et al. "Tracking Ca2+ ATPase intermediates in real time by x-ray solution scattering". Science Advances. 2020. 6(12). https://doi.org/10.1126/sciadv.aaz0981

Vancouver

Ravishankar H, Pedersen MN, Eklund M, Sitsel A, Li C, Duelli A et al. Tracking Ca2+ ATPase intermediates in real time by x-ray solution scattering. Science Advances. 2020 mar.;6(12):eaaz0981. doi: 10.1126/sciadv.aaz0981

Author

Ravishankar, Harsha ; Pedersen, Martin Nors ; Eklund, Mattias et al. / Tracking Ca2+ ATPase intermediates in real time by x-ray solution scattering. I: Science Advances. 2020 ; Bind 6, Nr. 12.

Bibtex

@article{133050c34ab94139ae11e770f54329e2,
title = "Tracking Ca2+ ATPase intermediates in real time by x-ray solution scattering",
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.",
keywords = "CA2+-ATPASE, CALCIUM-TRANSPORT, CONFORMATIONAL-CHANGES, MEMBRANE, MOLECULAR-DYNAMICS, PHOSPHOENZYME, PUMP, SARCOPLASMIC-RETICULUM, SKELETAL-MUSCLE, STRUCTURAL DYNAMICS",
author = "Harsha Ravishankar and Pedersen, {Martin Nors} and Mattias Eklund and Aljona Sitsel and Chenge Li and Annette Duelli and Matteo Levantino and Michael Wulff and Andreas Barth and Claus Olesen and Poul Nissen and Magnus Andersson",
year = "2020",
month = mar,
doi = "10.1126/sciadv.aaz0981",
language = "English",
volume = "6",
journal = "Science Advances",
issn = "2375-2548",
publisher = "American Association for the Advancement of Science",
number = "12",

}

RIS

TY - JOUR

T1 - Tracking Ca2+ ATPase intermediates in real time by x-ray solution scattering

AU - Ravishankar, Harsha

AU - Pedersen, Martin Nors

AU - Eklund, Mattias

AU - Sitsel, Aljona

AU - Li, Chenge

AU - Duelli, Annette

AU - Levantino, Matteo

AU - Wulff, Michael

AU - Barth, Andreas

AU - Olesen, Claus

AU - Nissen, Poul

AU - Andersson, Magnus

PY - 2020/3

Y1 - 2020/3

N2 - 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.

AB - 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.

KW - CA2+-ATPASE

KW - CALCIUM-TRANSPORT

KW - CONFORMATIONAL-CHANGES

KW - MEMBRANE

KW - MOLECULAR-DYNAMICS

KW - PHOSPHOENZYME

KW - PUMP

KW - SARCOPLASMIC-RETICULUM

KW - SKELETAL-MUSCLE

KW - STRUCTURAL DYNAMICS

UR - http://www.scopus.com/inward/record.url?scp=85082174090&partnerID=8YFLogxK

U2 - 10.1126/sciadv.aaz0981

DO - 10.1126/sciadv.aaz0981

M3 - Journal article

C2 - 32219166

AN - SCOPUS:85082174090

VL - 6

JO - Science Advances

JF - Science Advances

SN - 2375-2548

IS - 12

M1 - eaaz0981

ER -