The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum

Brandy L. Akin; Thomas D. Hurley; Zhenhui Chen; Larry R. Jones

doi:10.1074/jbc.M113.501585

The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum

Brandy L. Akin, Thomas D. Hurley, Zhenhui Chen, Larry R. Jones

Research output: Contribution to journal › Article

58 Scopus citations

Abstract

Background: Phospholamban (PLB) regulates sarco(endo)plasmic reticulum Ca²⁺-ATPase (SERCA) activity and is thus a key regulator of cardiac contractility. Results: We present the crystal structure of SERCA in complex with PLB at 2.8-A resolution. Conclusion: PLB stabilizes a divalent cation-free conformation of SERCA with collapsed Ca²⁺ binding sites. We call the structure E2-PLB. Significance: The E2-PLB structure explains how PLB decreases Ca²⁺ affinity and depresses cardiac contractility.

Original language	English (US)
Pages (from-to)	30181-30191
Number of pages	11
Journal	Journal of Biological Chemistry
Volume	288
Issue number	42
DOIs	https://doi.org/10.1074/jbc.M113.501585
State	Published - Oct 18 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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Akin, B. L., Hurley, T. D., Chen, Z., & Jones, L. R. (2013). The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum. Journal of Biological Chemistry, 288(42), 30181-30191. https://doi.org/10.1074/jbc.M113.501585

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abstract = "Background: Phospholamban (PLB) regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) activity and is thus a key regulator of cardiac contractility. Results: We present the crystal structure of SERCA in complex with PLB at 2.8-A resolution. Conclusion: PLB stabilizes a divalent cation-free conformation of SERCA with collapsed Ca2+ binding sites. We call the structure E2-PLB. Significance: The E2-PLB structure explains how PLB decreases Ca2+ affinity and depresses cardiac contractility.",

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AB - Background: Phospholamban (PLB) regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) activity and is thus a key regulator of cardiac contractility. Results: We present the crystal structure of SERCA in complex with PLB at 2.8-A resolution. Conclusion: PLB stabilizes a divalent cation-free conformation of SERCA with collapsed Ca2+ binding sites. We call the structure E2-PLB. Significance: The E2-PLB structure explains how PLB decreases Ca2+ affinity and depresses cardiac contractility.

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