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Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues

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  • Chikashi Toyoshima

    (The University of Tokyo)

  • Hiromi Nomura

    (National Institute for Physiological Sciences)

  • Takeo Tsuda

Abstract

P-type ion transporting ATPases are ATP-powered ion pumps that establish ion concentration gradients across biological membranes. Transfer of bound cations to the lumenal or extracellular side occurs while the ATPase is phosphorylated. Here we report at 2.3 Å resolution the structure of the calcium-ATPase of skeletal muscle sarcoplasmic reticulum, a representative P-type ATPase that is crystallized in the absence of Ca2+ but in the presence of magnesium fluoride, a stable phosphate analogue. This and other crystal structures determined previously provide atomic models for all four principal states in the reaction cycle. These structures show that the three cytoplasmic domains rearrange to move six out of ten transmembrane helices, thereby changing the affinity of the Ca2+-binding sites and the gating of the ion pathway. Release of ADP triggers the opening of the lumenal gate and release of phosphate its closure, effected mainly through movement of the A-domain, the actuator of transmembrane gates.

Suggested Citation

  • Chikashi Toyoshima & Hiromi Nomura & Takeo Tsuda, 2004. "Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues," Nature, Nature, vol. 432(7015), pages 361-368, November.
    • Handle: RePEc:nat:nature:v:432:y:2004:i:7015:d:10.1038_nature02981
    DOI: 10.1038/nature02981
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    Cited by:

    1. Nina Salustros & Christina Grønberg & Nisansala S. Abeyrathna & Pin Lyu & Fredrik Orädd & Kaituo Wang & Magnus Andersson & Gabriele Meloni & Pontus Gourdon, 2022. "Structural basis of ion uptake in copper-transporting P1B-type ATPases," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Hengjun Cui & Andreas U. Müller & Marc Leibundgut & Jiawen Tian & Nenad Ban & Eilika Weber-Ban, 2021. "Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation," Nature Communications, Nature, vol. 12(1), pages 1-12, December.

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