ArticleBiophysical journal2007
Side-chain protonation and mobility in the sarcoplasmic reticulum Ca2+-ATPase: implications for proton countertransport and Ca2+ release.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 33 citations in OpenAlex.
- Structural Basis for the Function of the C-Terminal Proton Release Pathway in the Calcium Pump.International journal of molecular sciences · 2021Article
- Linking Biochemical and Structural States of SERCA: Achievements, Challenges, and New Opportunities.International journal of molecular sciences · 2020Review
- Proton Countertransport and Coupled Gating in the Sarcoplasmic Reticulum Calcium Pump.Journal of molecular biology · 2018Article
- Preexisting domain motions underlie protonation-dependent structural transitions of the P-type CaPhysical chemistry chemical physics : PCCP · 2017Article
- The CaMolecular bioSystems · 2017Review
- Dipole-Potential-Mediated Effects on Ion Pump Kinetics.Biophysical journal · 2015Review
- Hofmeister effect of anions on calcium translocation by sarcoplasmic reticulum Ca(2+)-ATPase.Scientific reports · 2015Article
- Protonation of key acidic residues is critical for the K⁺-selectivity of the Na/K pump.Nature structural & molecular biology · 2011Article
- Article
- Identification of functionally segregated sarcoplasmic reticulum calcium stores in pulmonary arterial smooth muscle.The Journal of biological chemistry · 2010Article
- High-yield heterologous expression of wild type and mutant Ca(2+) ATPase: Characterization of Ca(2+) binding sites by charge transfer.Journal of molecular biology · 2009Article
- Coefficients for active transport and thermogenesis of Ca2+-ATPase isoforms.Biophysical journal · 2009Article
- Is the Ca2+-ATPase from sarcoplasmic reticulum also a heat pump?European biophysics journal : EBJ · 2008Article
- Specificity of ligand binding to transport sites: Ca2+ binding to the Ca2+ transport ATPase and its dependence on H+ and Mg2+.Archives of biochemistry and biophysics · 2008Article
- Protonation and hydrogen bonding of Ca2+ site residues in the E2P phosphoenzyme intermediate of sarcoplasmic reticulum Ca2+-ATPase studied by a combination of infrared spectroscopy and electrostatic calculations.Biophysical journal · 2008Article
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protonation of acidic residues in the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA 1a) was studied by multiconformation continuum electrostatic calculations in the Ca(2+)-bound state Ca(2)E1, in the Ca(2+)-free state E2(TG) with bound thapsigargin, and in the E2P (ADP-insensitive phosphoenzyme) analog state with MgF(4)(2-) E2(TG+MgF(4)(2-)). Around physiological pH, all acidic Ca(2+) ligands (Glu(309), Glu(771), Asp(800), and Glu(908)) were unprotonated in Ca(2)E1; in E2(TG) and E2(TG+MgF(4)(2-)) Glu(771), Asp(800), and Glu(908) were protonated. Glu(771) and Glu(908) had calculated pK(a) values larger than 14 in E2(TG) and E2(TG+MgF(4)(2-)), whereas Asp(800) titrated with calculated pK(a) values near 7.5. Glu(309) had very different pK(a) values in the Ca(2+)-free states: 8.4 in E2(TG+MgF(4)(2-)) and 4.7 in E2(TG) because of a different local backbone conformation. This indicates that Glu(309) can switch between a high and a low pK(a) mode, depending on the local backbone conformation. Protonated Glu(309) occupied predominantly two main, very differently orientated side-chain conformations in E2(TG+MgF(4)(2-)): one oriented inward toward the other Ca(2+) ligands and one oriented outward toward a protein channel that seems to be in contact with the cytoplasm. Upon deprotonation, Glu(309) adopted completely the outwardly orientated side-chain conformation. The contact of Glu(309) with the cytoplasm in E2(TG+MgF(4)(2-)) makes this residue unlikely to bind lumenal protons. Instead it might serve as a proton shuttle between Ca(2+)-binding site I and the cytoplasm. Glu(771), Asp(800), and Glu(908) are proposed to take part in proton countertransport.
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