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Claus Elsborg Olesen

Cyclopiazonic Acid Is Complexed to a Divalent Metal Ion When Bound to the Sarcoplasmic Reticulum Ca2+-ATPase

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Standard

Cyclopiazonic Acid Is Complexed to a Divalent Metal Ion When Bound to the Sarcoplasmic Reticulum Ca2+-ATPase. / Laursen, Mette; Bublitz, Maike; Moncoq, Karine; Olesen, Claus; Møller, Jesper Vuust; Young, Howard; Nissen, Poul; Morth, Jens Preben.

I: Journal of Biological Chemistry, Bind 284, Nr. 20, 15.06.2009, s. 13513-13518.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Laursen, M, Bublitz, M, Moncoq, K, Olesen, C, Møller, JV, Young, H, Nissen, P & Morth, JP 2009, 'Cyclopiazonic Acid Is Complexed to a Divalent Metal Ion When Bound to the Sarcoplasmic Reticulum Ca2+-ATPase', Journal of Biological Chemistry, bind 284, nr. 20, s. 13513-13518.

APA

Laursen, M., Bublitz, M., Moncoq, K., Olesen, C., Møller, J. V., Young, H., Nissen, P., & Morth, J. P. (2009). Cyclopiazonic Acid Is Complexed to a Divalent Metal Ion When Bound to the Sarcoplasmic Reticulum Ca2+-ATPase. Journal of Biological Chemistry, 284(20), 13513-13518.

CBE

Laursen M, Bublitz M, Moncoq K, Olesen C, Møller JV, Young H, Nissen P, Morth JP. 2009. Cyclopiazonic Acid Is Complexed to a Divalent Metal Ion When Bound to the Sarcoplasmic Reticulum Ca2+-ATPase. Journal of Biological Chemistry. 284(20):13513-13518.

MLA

Laursen, Mette o.a.. "Cyclopiazonic Acid Is Complexed to a Divalent Metal Ion When Bound to the Sarcoplasmic Reticulum Ca2+-ATPase". Journal of Biological Chemistry. 2009, 284(20). 13513-13518.

Vancouver

Laursen M, Bublitz M, Moncoq K, Olesen C, Møller JV, Young H o.a. Cyclopiazonic Acid Is Complexed to a Divalent Metal Ion When Bound to the Sarcoplasmic Reticulum Ca2+-ATPase. Journal of Biological Chemistry. 2009 jun. 15;284(20):13513-13518.

Author

Laursen, Mette ; Bublitz, Maike ; Moncoq, Karine ; Olesen, Claus ; Møller, Jesper Vuust ; Young, Howard ; Nissen, Poul ; Morth, Jens Preben. / Cyclopiazonic Acid Is Complexed to a Divalent Metal Ion When Bound to the Sarcoplasmic Reticulum Ca2+-ATPase. I: Journal of Biological Chemistry. 2009 ; Bind 284, Nr. 20. s. 13513-13518.

Bibtex

@article{dec6c5e09bdd11dea092000ea68e967b,
title = "Cyclopiazonic Acid Is Complexed to a Divalent Metal Ion When Bound to the Sarcoplasmic Reticulum Ca2+-ATPase",
abstract = "Abstract: We have determined the structure of the sarco(endo) plasmic reticulum Ca2+-ATPase (SERCA) in an E2.P-i-like form stabilized as a complex with MgF42-, an ATP analog, adenosine 5'-(beta,gamma-methylene) triphosphate (AMPPCP), and cyclopiazonic acid (CPA). The structure determined at 2.5 angstrom resolution leads to a significantly revised model of CPA binding when compared with earlier reports. It shows that a divalent metal ion is required for CPA binding through coordination of the tetramic acid moiety at a characteristic kink of the M1 helix found in all P-type ATPase structures, which is expected to be part of the cytoplasmic cation access pathway. Our model is consistent with the biochemical data on CPA function and provides new measures in structure-based drug design targeting Ca2+-ATPases, e. g. from pathogens. We also present an extended structural basis of ATP modulation pinpointing key residues at or near the ATP binding site. A structural comparison to the Na+, K+-ATPase reveals that the Phe(93) side chain occupies the equivalent binding pocket of the CPA site in SERCA, suggesting an important role of this residue in stabilization of the potassium-occluded E2 state of Na+, K+-ATPase.",
author = "Mette Laursen and Maike Bublitz and Karine Moncoq and Claus Olesen and M{\o}ller, {Jesper Vuust} and Howard Young and Poul Nissen and Morth, {Jens Preben}",
year = "2009",
month = jun,
day = "15",
language = "English",
volume = "284",
pages = "13513--13518",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "20",

}

RIS

TY - JOUR

T1 - Cyclopiazonic Acid Is Complexed to a Divalent Metal Ion When Bound to the Sarcoplasmic Reticulum Ca2+-ATPase

AU - Laursen, Mette

AU - Bublitz, Maike

AU - Moncoq, Karine

AU - Olesen, Claus

AU - Møller, Jesper Vuust

AU - Young, Howard

AU - Nissen, Poul

AU - Morth, Jens Preben

PY - 2009/6/15

Y1 - 2009/6/15

N2 - Abstract: We have determined the structure of the sarco(endo) plasmic reticulum Ca2+-ATPase (SERCA) in an E2.P-i-like form stabilized as a complex with MgF42-, an ATP analog, adenosine 5'-(beta,gamma-methylene) triphosphate (AMPPCP), and cyclopiazonic acid (CPA). The structure determined at 2.5 angstrom resolution leads to a significantly revised model of CPA binding when compared with earlier reports. It shows that a divalent metal ion is required for CPA binding through coordination of the tetramic acid moiety at a characteristic kink of the M1 helix found in all P-type ATPase structures, which is expected to be part of the cytoplasmic cation access pathway. Our model is consistent with the biochemical data on CPA function and provides new measures in structure-based drug design targeting Ca2+-ATPases, e. g. from pathogens. We also present an extended structural basis of ATP modulation pinpointing key residues at or near the ATP binding site. A structural comparison to the Na+, K+-ATPase reveals that the Phe(93) side chain occupies the equivalent binding pocket of the CPA site in SERCA, suggesting an important role of this residue in stabilization of the potassium-occluded E2 state of Na+, K+-ATPase.

AB - Abstract: We have determined the structure of the sarco(endo) plasmic reticulum Ca2+-ATPase (SERCA) in an E2.P-i-like form stabilized as a complex with MgF42-, an ATP analog, adenosine 5'-(beta,gamma-methylene) triphosphate (AMPPCP), and cyclopiazonic acid (CPA). The structure determined at 2.5 angstrom resolution leads to a significantly revised model of CPA binding when compared with earlier reports. It shows that a divalent metal ion is required for CPA binding through coordination of the tetramic acid moiety at a characteristic kink of the M1 helix found in all P-type ATPase structures, which is expected to be part of the cytoplasmic cation access pathway. Our model is consistent with the biochemical data on CPA function and provides new measures in structure-based drug design targeting Ca2+-ATPases, e. g. from pathogens. We also present an extended structural basis of ATP modulation pinpointing key residues at or near the ATP binding site. A structural comparison to the Na+, K+-ATPase reveals that the Phe(93) side chain occupies the equivalent binding pocket of the CPA site in SERCA, suggesting an important role of this residue in stabilization of the potassium-occluded E2 state of Na+, K+-ATPase.

M3 - Journal article

VL - 284

SP - 13513

EP - 13518

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 20

ER -