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Modulatory and catalytic modes of ATP binding by the calcium pump.

Jensen AM, Sørensen TL, Olesen C, Møller JV, Nissen P
EMBO J 25 2305-14 (2006)
Related entries: 2c88, 2c8l, 2c9m

Cited: 115 times
EuropePMC logo PMID: 16710301

Abstract

We present crystal structures of the calcium-free E2 state of the sarcoplasmic reticulum Ca2+ -ATPase, stabilized by the inhibitor thapsigargin and the ATP analog AMPPCP. The structures allow us to describe the ATP binding site in a modulatory mode uncoupled from the Asp351 phosphorylation site. The Glu439 side chain interacts with AMPPCP via an Mg2+ ion in accordance with previous Fe2+ -cleavage studies implicating this residue in the ATPase cycle and in magnesium binding. Functional data on Ca2+ mediated activation indicate that the crystallized state represents an initial stage of ATP modulated deprotonation of E2, preceding the binding of Ca2+ ions in the membrane from the cytoplasmic side. We propose a mechanism of Ca2+ activation of phosphorylation leading directly from the compact E2-ATP form to the Ca2E1-ATP state. In addition, a role of Glu439 in ATP modulation of other steps of the functional cycle is suggested.

Reviews - 2c8k mentioned but not cited (1)

  1. Lipid interaction sites on channels, transporters and receptors: Recent insights from molecular dynamics simulations. Hedger G, Sansom MSP. Biochim Biophys Acta 1858 2390-2400 (2016)

Articles - 2c8k mentioned but not cited (10)

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