Contributors: Moscow Institute of Physics and Technology Moscow (MIPT); Institute of Complex Systems (ICS); Forschungszentrum Jülich GmbH; Helmholtz-Gemeinschaft = Helmholtz Association-Helmholtz-Gemeinschaft = Helmholtz Association; European X-ray Free Electron Laser GmbH; Structural Biology Brussels (SBB); Vrije Universiteit Brussel (VUB); Institut de biologie structurale (IBS - UMR 5075); Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG); Direction de Recherche Fondamentale (CEA) (DRF (CEA)); Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)); Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA); DESY, European Mol Biol Lab, D-22607 Hamburg, Germany; Institute of Biological Information Processing Jülich (IBI-7); Institute for Biophysical Chemistry; Medizinische Hochschule Hannover = Hannover Medical School (MHH); Jülich Center for Structural Biology Jülich (JuStruct); Research Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow; Institut für Physikalische Biologie Düsseldorfd; Heinrich Heine Universität Düsseldorf = Heinrich Heine University Düsseldorf; Max Planck Institute of Molecular Physiology; Max-Planck-Gesellschaft; Department of Structural Biology, Max-Planck-Institute of Biophysics, Frankfurt, Germany; ANR-17-EURE-0003,CBH-EUR-GS,CBH-EUR-GS(2017)
نبذة مختصرة : International audience ; Hydrogen bonds are fundamental to the structure and function of biological macromolecules and have been explored in detail. The chains of hydrogen bonds (CHBs) and low-barrier hydrogen bonds (LBHBs) were proposed to play essential roles in enzyme catalysis and proton transport. However, high-resolution structural data from CHBs and LBHBs is limited. The challenge is that their 'visualization' requires ultrahigh-resolution structures of the ground and functionally important intermediate states to identify proton translocation events and perform their structural assignment. Our true-atomic-resolution structures of the light-driven proton pump bacteriorhodopsin, a model in studies of proton transport, show that CHBs and LBHBs not only serve as proton pathways, but also are indispensable for long-range communications, signaling and proton storage in proteins. The complete picture of CHBs and LBHBs discloses their multifunctional roles in providing protein functions and presents a consistent picture of proton transport and storage resolving long-standing debates and controversies.
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