DOI: 10.1126/science.1106289. Dephosphorylation of the Calcium Pump Coupled to Counterion Occlusion

Dephosphorylation of the Calcium Pump Coupled to Counterion Occlusion

10.1126/science.1106289

Crossref journal-article

American Association for the Advancement of Science (AAAS)

Science (221)

Abstract

P-type ATPases extract energy by hydrolysis of adenosine triphosphate (ATP) in two steps, formation and breakdown of a covalent phosphoenzyme intermediate. This process drives active transport and countertransport of the cation pumps. We have determined the crystal structure of rabbit sarcoplasmic reticulum Ca 2+ adenosine triphosphatase in complex with aluminum fluoride, which mimics the transition state of hydrolysis of the counterion-bound (protonated) phosphoenzyme. On the basis of structural analysis and biochemical data, we find this form to represent an occluded state of the proton counterions. Hydrolysis is catalyzed by the conserved Thr-Gly-Glu-Ser motif, and it exploits an associative nucleophilic reaction mechanism of the same type as phosphoryl transfer from ATP. On this basis, we propose a general mechanism of occluded transition states of Ca 2+ transport and H + countertransport coupled to phosphorylation and dephosphorylation, respectively.

Bibliography

Olesen, C., SÃ¸rensen, T. L.-M., Nielsen, R. C., MÃ¸ller, J. V., & Nissen, P. (2004). Dephosphorylation of the Calcium Pump Coupled to Counterion Occlusion. Science, 306(5705), 2251â2255.

Authors 5

Claus Olesen (first)
Thomas Lykke-Møller Sørensen (additional)
Rikke Christina Nielsen (additional)
Jesper Vuust Møller (additional)
Poul Nissen (additional)

References 29 Referenced 240

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Materials and methods are available as supporting material on Science Online.
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B. Forbush III, I. Klodos, in The Sodium Pump: Structure, Mechanism, and Regulation, J. H. Kaplan, P. de Weer, Eds. (Rockefeller Univ. Press, New York, 1991), pp. 211. / The Sodium Pump: Structure, Mechanism, and Regulation (1991)
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We thank B. Holm B. Nielsen and C. Lauridsen for expert technical assistance; the staff at the Protein Structure Factory beamline BL14.1 of Free University Berlin at Berliner Elektronenspeicherring-Gesellschaft für Synchrotronstrahlung m. b. H. the staff at European Synchrotron Radiation Facility (ESRF) beamline ID29; J. L. Karlsen and R. Jørgensen for extensive computer support; and J. Nyborg for fruitful scientific discussions. This work was supported by an Ole Rømer Research grant; the Center for Structural Biology; the Dansync program under the Danish Natural Science Research Council; a grant from the Lundbeck Foundation (P.N.) and grants from the Danish Medical Research Council Aarhus University Research Foundation and Novo Nordic Foundation (J.V.M.). Coordinates and structure-factor amplitudes have been deposited to the Protein Data Bank under code 1XP5.

Dates

Type	When
Created	20 years, 7 months ago (Dec. 26, 2004, 11:34 p.m.)
Deposited	1 year, 7 months ago (Jan. 9, 2024, 10:58 p.m.)
Indexed	3 weeks, 1 day ago (Aug. 2, 2025, 12:42 a.m.)
Issued	20 years, 8 months ago (Dec. 24, 2004)
Published	20 years, 8 months ago (Dec. 24, 2004)
Published Print	20 years, 8 months ago (Dec. 24, 2004)

Funders 0

None

BibTeX

@article{Olesen_2004, title={Dephosphorylation of the Calcium Pump Coupled to Counterion Occlusion}, volume={306}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.1106289}, DOI={10.1126/science.1106289}, number={5705}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Olesen, Claus and Sørensen, Thomas Lykke-Møller and Nielsen, Rikke Christina and Møller, Jesper Vuust and Nissen, Poul}, year={2004}, month=dec, pages={2251–2255} }

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