Atomic view of the histidine environment stabilizing higher-pH conformations of pH-dependent proteins

Céline Valéry, Stéphanie Deville-Foillard, Christelle Lefebvre, Nuria Taberner, Pierre Legrand, Florian Meneau, Cristelle Meriadec, Camille Delvaux, Thomas Bizien, Emmanouil Kasotakis, Carmen Lopez-Iglesias, Andrew Gall, Stéphane Bressanelli, Marie-Hélène Le Du, Maïté Paternostre () and Franck Artzner ()
Additional contact information
Céline Valéry: Biomolecular Interaction Centre, School of Biological Sciences, University of Canterbury
Stéphanie Deville-Foillard: Ipsen
Christelle Lefebvre: CNRS, UMR 6251, Institut de Physique de Rennes, 263 av. Général Leclerc, Université Rennes I
Nuria Taberner: Ipsen
Pierre Legrand: Synchrotron SOLEIL
Florian Meneau: Synchrotron SOLEIL
Cristelle Meriadec: CNRS, UMR 6251, Institut de Physique de Rennes, 263 av. Général Leclerc, Université Rennes I
Camille Delvaux: CEA, Institute of Biology and Technologies of Saclay
Thomas Bizien: CNRS, UMR 6251, Institut de Physique de Rennes, 263 av. Général Leclerc, Université Rennes I
Emmanouil Kasotakis: CEA, Institute of Biology and Technologies of Saclay
Carmen Lopez-Iglesias: Cryo-Electron Microscopy Unit. Scientific and Tecnological Centers of the University of Barcelona
Andrew Gall: CEA, Institute of Biology and Technologies of Saclay
Stéphane Bressanelli: CEA, Institute of Biology and Technologies of Saclay
Marie-Hélène Le Du: CEA, Institute of Biology and Technologies of Saclay
Maïté Paternostre: CEA, Institute of Biology and Technologies of Saclay
Franck Artzner: CNRS, UMR 6251, Institut de Physique de Rennes, 263 av. Général Leclerc, Université Rennes I

Nature Communications, 2015, vol. 6, issue 1, 1-8

Abstract: Abstract External stimuli are powerful tools that naturally control protein assemblies and functions. For example, during viral entry and exit changes in pH are known to trigger large protein conformational changes. However, the molecular features stabilizing the higher pH structures remain unclear. Here we elucidate the conformational change of a self-assembling peptide that forms either small or large nanotubes dependent on the pH. The sub-angstrom high-pH peptide structure reveals a globular conformation stabilized through a strong histidine-serine H-bond and a tight histidine-aromatic packing. Lowering the pH induces histidine protonation, disrupts these interactions and triggers a large change to an extended β-sheet-based conformation. Re-visiting available structures of proteins with pH-dependent conformations reveals both histidine-containing aromatic pockets and histidine-serine proximity as key motifs in higher pH structures. The mechanism discovered in this study may thus be generally used by pH-dependent proteins and opens new prospects in the field of nanomaterials.

Date: 2015
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DOI: 10.1038/ncomms8771

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