Angle change of the A-domain in a single SERCA1a molecule detected by defocused orientation imaging View Full Text


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Article Info

DATE

2021-07-01

AUTHORS

Takanobu A. Katoh, Takashi Daiho, Kazuo Yamasaki, Stefania Danko, Shoko Fujimura, Hiroshi Suzuki

ABSTRACT

The sarcoendoplasmic reticulum Ca2+-ATPase (SERCA) transports Ca2+ ions across the membrane coupled with ATP hydrolysis. Crystal structures of ligand-stabilized molecules indicate that the movement of actuator (A) domain plays a crucial role in Ca2+ translocation. However, the actual structural movements during the transitions between intermediates remain uncertain, in particular, the structure of E2PCa2 has not been solved. Here, the angle of the A-domain was measured by defocused orientation imaging using isotropic total internal reflection fluorescence microscopy. A single SERCA1a molecule, labeled with fluorophore ReAsH on the A-domain in fixed orientation, was embedded in a nanodisc, and stabilized on Ni–NTA glass. Activation with ATP and Ca2+ caused angle changes of the fluorophore and therefore the A-domain, motions lost by inhibitor, thapsigargin. Our high-speed set-up captured the motion during EP isomerization, and suggests that the A-domain rapidly rotates back and forth from an E1PCa2 position to a position close to the E2P state. This is the first report of the detection in the movement of the A-domain as an angle change. Our method provides a powerful tool to investigate the conformational change of a membrane protein in real-time. More... »

PAGES

13672

References to SciGraph publications

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  • 2017-01-24. Membrane Perturbation of ADP-insensitive Phosphoenzyme of Ca2+-ATPase Modifies Gathering of Transmembrane Helix M2 with Cytoplasmic Domains and Luminal Gating in SCIENTIFIC REPORTS
  • 2019-05-15. Single-molecule pull-out manipulation of the shaft of the rotary motor F1-ATPase in SCIENTIFIC REPORTS
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  • 2017-11-08. Dynamics of P-type ATPase transport revealed by single-molecule FRET in NATURE
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/s41598-021-92986-3

    DOI

    http://dx.doi.org/10.1038/s41598-021-92986-3

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1139277666

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/34211016


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