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

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

Research output: Contribution to journal › Article

50 Citations (Scopus)

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 languageEnglish
Pages (from-to)30181-30191
Number of pages11
JournalJournal of Biological Chemistry
Volume288
Issue number42
DOIs
StatePublished - Oct 18 2013

Fingerprint

Sarcoplasmic Reticulum
Pumps
Calcium
Reticulum
Calcium-Transporting ATPases
Divalent Cations
Conformations
phospholamban
Crystal structure
Binding Sites

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum. / Akin, Brandy L.; Hurley, Thomas; Chen, Zhenhui; Jones, Larry.

In: Journal of Biological Chemistry, Vol. 288, No. 42, 18.10.2013, p. 30181-30191.

Research output: Contribution to journal › Article

Akin, BL, Hurley, T, Chen, Z & Jones, L 2013, 'The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum', Journal of Biological Chemistry, vol. 288, no. 42, pp. 30181-30191. https://doi.org/10.1074/jbc.M113.501585
Akin BL, Hurley T, Chen Z, Jones L. The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum. Journal of Biological Chemistry. 2013 Oct 18;288(42):30181-30191. https://doi.org/10.1074/jbc.M113.501585
Akin, Brandy L. ; Hurley, Thomas ; Chen, Zhenhui ; Jones, Larry. / The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum. In: Journal of Biological Chemistry. 2013 ; Vol. 288, No. 42. pp. 30181-30191.
@article{5db1a9983d2d4239a4de56442cb20906,
title = "The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum",
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.",
author = "Akin, {Brandy L.} and Thomas Hurley and Zhenhui Chen and Larry Jones",
year = "2013",
month = "10",
day = "18",
doi = "10.1074/jbc.M113.501585",
language = "English",
volume = "288",
pages = "30181--30191",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "42",

}

TY - JOUR

T1 - The structural basis for phospholamban inhibition of the calcium pump in sarcoplasmic reticulum

AU - Akin, Brandy L.

AU - Hurley, Thomas

AU - Chen, Zhenhui

AU - Jones, Larry

PY - 2013/10/18

Y1 - 2013/10/18

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=84885968069&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84885968069&partnerID=8YFLogxK

U2 - 10.1074/jbc.M113.501585

DO - 10.1074/jbc.M113.501585

M3 - Article

VL - 288

SP - 30181

EP - 30191

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 42

ER -

Access to Document