Conformation of a Peptide Encompassing the Proton Translocation Channel of Vacuolar H+-ATPase
Copyright policy )Conformation of a Peptide Encompassing the Proton Translocation Channel of Vacuolar H+-ATPase
The structural properties of a crucial transmembrane helix for proton translocation in vacuolar ATPase are studied using double site-directed spin-labeling combined with electron spin resonance (ESR) (or electron paramagnetic resonance) and circular dichroism spectroscopy in sodium dodecyl sulfate micelles. For this purpose, we use a synthetic peptide derived from transmembrane helix 7 of subunit a from the yeast Saccharomyces cerevisiae vacuolar proton-translocating ATPase that contains two natural cysteine residues suitable for spin-labeling. The interspin distance is calculated using a second-moment analysis of the methanethiosulfonate spin-label ESR spectra at 150 K. Molecular dynamics simulation is used to study the effect of the side-chain dynamics and backbone dynamics on the interspin distance. Based on the combined results from ESR, circular dichroism, and molecular dynamics simulation we conclude that the peptide forms a dynamic alpha-helix. We discuss this finding in the light of current models for proton translocation. A novel role for a buried charged residue (H729) is proposed.
- Wageningen University & Research Netherlands
- WAGENINGEN UNIVERSITY Netherlands
- Université Wageningen Netherlands
Vacuolar Proton-Translocating ATPases, Protein Conformation, receptor, domain, Molecular Sequence Data, Biophysics, Molecular Conformation, coiled-coils, Saccharomyces cerevisiae, Protein Structure, Secondary, molecular-dynamics simulations, alpha-helix, subunit, Amino Acid Sequence, Adenosine Triphosphatases, pi-helix, Circular Dichroism, electron-spin-resonance, Electron Spin Resonance Spectroscopy, Temperature, Biological Transport, yeast v-atpase, Protons, protein, Peptides
Vacuolar Proton-Translocating ATPases, Protein Conformation, receptor, domain, Molecular Sequence Data, Biophysics, Molecular Conformation, coiled-coils, Saccharomyces cerevisiae, Protein Structure, Secondary, molecular-dynamics simulations, alpha-helix, subunit, Amino Acid Sequence, Adenosine Triphosphatases, pi-helix, Circular Dichroism, electron-spin-resonance, Electron Spin Resonance Spectroscopy, Temperature, Biological Transport, yeast v-atpase, Protons, protein, Peptides
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