Critical Roles of Interdomain Interactions for Modulatory ATP Binding to Sarcoplasmic Reticulum Ca2+-ATPase

Clausen, Johannes; Holdensen, Anne Nyholm; Andersen, Jens Peter

doi:10.1074/jbc.m114.571687

Cited by 5 publications

(2 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This effect of ATP on the dephosphorylation reaction is reversed when residues bridging the A and N domains in E2∼P are mutated. That is, the E2P ground state becomes relatively more stabilized by ATP than E2∼P, and the dephosphorylation reaction is slowed down ( 19 , 20 ).…”

Section: Resultsmentioning

confidence: 99%

Cryoelectron microscopy of Na ⁺ ,K ⁺ -ATPase in the two E2P states with and without cardiotonic steroids

Kanai

Cornelius

Vilsen

et al. 2022

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Significance The E2P state of Na + ,K + -ATPase, in which the ATPase is phosphorylated and of low affinity to Na + with the extracellular gate opened, shows different biochemical properties depending on whether the phosphate is transferred from ATP in the forward reaction or from inorganic phosphate (P i ) in the backward reaction. We present here cryoelectron microscopy structures of Na + ,K + -ATPase in the two E2P states, explaining their different biochemical properties established a half century ago. The new electron microscopy maps show previously unseen structural features, including unexpected binding modes of cardiotonic steroids, specific and medically important inhibitors of the ATPase, and stabilization by ATP of the E2P state.

show abstract

Section: Resultsmentioning

confidence: 99%

Cryoelectron microscopy of Na ⁺ ,K ⁺ -ATPase in the two E2P states with and without cardiotonic steroids

Kanai

Cornelius

Vilsen

et al. 2022

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…While the SERCA1 ATP-binding site flips between the catalytic (Ca 2+ E1-ATP) and modulatory (E2-ATP) mode (Jensen et al 2006;Clausen et al 2011; Aguayo-Ortiz and Espinoza-Fonseca 2020; Kabashima et al 2020), ATP serves as an interdomain-interaction mediator at various stages of the transport cycle. The majority of amino acid residues involved in ATP binding are almost identical for both the E1 and E2 conformation (Autry et al 2012;Clausen et al 2014;Páez-Pérez et al 2016;de la Cruz-Torres et al 2020).…”

Section: E1mentioning

confidence: 99%

Interaction of quercetin and its derivatives with Ca2+-ATPase from sarcoplasmic reticulum: Kinetic and molecular modeling studies

Rezbarikova,

Viskupicova,

Majekova

et al. 2023

gpb

View full text Add to dashboard Cite

Sarcoplasmic reticulum Ca 2+ -ATPases (SERCAs) regulate cellular calcium homeostasis and are targeted for age-related diseases. Among 14 SERCA mRNA splice variants, SERCA1a is specific to adult fast-twitch skeletal muscle. Quercetin derivatives (monochloropivaloylquercetin (CPQ), IC 50 = 195.7 µM; 2-chloro-1,4-naphthoquinonequercetin (CHNQ), IC 50 = 60.3 µM) were studied for their impact on SERCA1a using molecular modeling and enzyme kinetics. While there were some similarities in kinetic parameters and molecular modeling, the compounds exhibited diverse actions on SERCA1a. Quercetin reduced activity by 48% at 250 μM by binding to the cytosolic ATP-binding pocket with increased ATP affinity. CPQ bound near the Ca 2+ -binding site, possibly altering the transmembrane domain. CHNQ significantly reduced activity by 94% at 250 μM without binding to substrate sites. It was proposed that CHNQ induced global protein structure changes, inhibiting Ca 2+ -ATPase activity.

show abstract

Determination of the ATP Affinity of the Sarcoplasmic Reticulum Ca2+-ATPase by Competitive Inhibition of [γ-32P]TNP-8N3-ATP Photolabeling

et al. 2016

View full text Add to dashboard Cite

The photoactivation of aryl azides is commonly employed as a means to covalently attach cross-linking and labeling reagents to proteins, facilitated by the high reactivity of the resultant aryl nitrenes with amino groups present in the protein side chains. We have developed a simple and reliable assay for the determination of the ATP binding affinity of native or recombinant sarcoplasmic reticulum Ca(2+)-ATPase, taking advantage of the specific photolabeling of Lys(492) in the Ca(2+)-ATPase by [γ-(32)P]2',3'-O-(2,4,6-trinitrophenyl)-8-azido-adenosine 5'-triphosphate ([γ-(32)P]TNP-8N3-ATP) and the competitive inhibition by ATP of the photolabeling reaction. The method allows determination of the ATP affinity of Ca(2+)-ATPase mutants expressed in mammalian cell culture in amounts too minute for conventional equilibrium binding studies. Here, we describe the synthesis and purification of the [γ-(32)P]TNP-8N3-ATP photolabel, as well as its application in ATP affinity measurements.

show abstract

Critical Roles of Interdomain Interactions for Modulatory ATP Binding to Sarcoplasmic Reticulum Ca2+-ATPase

Cited by 5 publications

References 50 publications

Cryoelectron microscopy of Na ⁺ ,K ⁺ -ATPase in the two E2P states with and without cardiotonic steroids

Cryoelectron microscopy of Na ⁺ ,K ⁺ -ATPase in the two E2P states with and without cardiotonic steroids

Interaction of quercetin and its derivatives with Ca2+-ATPase from sarcoplasmic reticulum: Kinetic and molecular modeling studies

Determination of the ATP Affinity of the Sarcoplasmic Reticulum Ca2+-ATPase by Competitive Inhibition of [γ-32P]TNP-8N3-ATP Photolabeling

Contact Info

Product

Resources

About

Critical Roles of Interdomain Interactions for Modulatory ATP Binding to Sarcoplasmic Reticulum Ca2+-ATPase

Cited by 5 publications

References 50 publications

Cryoelectron microscopy of Na + ,K + -ATPase in the two E2P states with and without cardiotonic steroids

Cryoelectron microscopy of Na + ,K + -ATPase in the two E2P states with and without cardiotonic steroids

Interaction of quercetin and its derivatives with Ca2+-ATPase from sarcoplasmic reticulum: Kinetic and molecular modeling studies

Determination of the ATP Affinity of the Sarcoplasmic Reticulum Ca2+-ATPase by Competitive Inhibition of [γ-32P]TNP-8N3-ATP Photolabeling

Contact Info

Product

Resources

About

Cryoelectron microscopy of Na ⁺ ,K ⁺ -ATPase in the two E2P states with and without cardiotonic steroids

Cryoelectron microscopy of Na ⁺ ,K ⁺ -ATPase in the two E2P states with and without cardiotonic steroids