Nature Structural and Molecular Biology, volume 29, issue 5, pages 440-450
True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins
Borshchevskiy Valentin
1, 2, 3
,
Kovalev Kirill
4
,
Round Ekaterina
5
,
Efremov Rouslan G.
6, 7
,
Astashkin Roman
2, 8
,
Bourenkov Gleb
4
,
Bratanov Dmitry
1, 3
,
Balandin Taras
1, 3
,
Chizhov Igor
9
,
Baeken Christian
1, 3
,
Gushchin Ivan
2
,
Kuzmin Alexander
2
,
Alekseev Alexey
2
,
Rogachev Andrey
2, 10
,
RAABE Dierk
1, 3, 11
,
ENGELHARD MARTIN
12
,
Bamberg Ernst
13
,
Büldt Georg
2
,
Gordeliy Valentin
1, 2, 3, 8
1
JuStruct: Jülich Center for Structural Biology, Forschungszentrum Jülich, Jülich, Germany
|
3
Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany
|
4
European Molecular Biology Laboratory, Hamburg unit c/o DESY, Hamburg, Germany
|
5
European X-Ray Free Electron Laser GmbH, Schenefeld, Germany
|
6
Structural Biology Brussels, Department of Bioengineering Sciences, Vrije Universiteit Brussel, Brussels, Belgium
|
9
Institute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany
|
11
Institut für physikalische Biologie, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany
|
12
Department of Structural Biochemistry, Max Planck Institute for Physiology, Dortmund, Germany
|
13
Max Planck Institute of Biophysics, Frankfurt am Main, Germany
|
Publication type: Journal Article
Publication date: 2022-04-28
Quartile SCImago
Q1
Quartile WOS
Q1
Impact factor: 16.8
ISSN: 15459993, 15459985
Molecular Biology
Structural Biology
Abstract
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. High-resolution (≤1.2 Å) structures of functional states of bacteriorhodopsin reveal the molecular mechanism for generating a membrane proton electrochemical gradient, a key event of cell bioenergetics driving ATP synthesis.
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1
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Borshchevskiy V. et al. True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins // Nature Structural and Molecular Biology. 2022. Vol. 29. No. 5. pp. 440-450.
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Borshchevskiy V., Kovalev K., Round E., Efremov R. G., Astashkin R., Bourenkov G., Bratanov D., Balandin T., Chizhov I., Baeken C., Gushchin I., Kuzmin A., Alekseev A., Rogachev A., RAABE D., ENGELHARD M., Bamberg E., Büldt G., Gordeliy V. True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins // Nature Structural and Molecular Biology. 2022. Vol. 29. No. 5. pp. 440-450.
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TY - JOUR
DO - 10.1038/s41594-022-00762-2
UR - https://doi.org/10.1038%2Fs41594-022-00762-2
TI - True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins
T2 - Nature Structural and Molecular Biology
AU - Borshchevskiy, Valentin
AU - Kovalev, Kirill
AU - Round, Ekaterina
AU - Efremov, Rouslan G.
AU - Astashkin, Roman
AU - Bourenkov, Gleb
AU - Bratanov, Dmitry
AU - Balandin, Taras
AU - Chizhov, Igor
AU - Baeken, Christian
AU - Gushchin, Ivan
AU - Kuzmin, Alexander
AU - Alekseev, Alexey
AU - Rogachev, Andrey
AU - RAABE, Dierk
AU - ENGELHARD, MARTIN
AU - Bamberg, Ernst
AU - Büldt, Georg
AU - Gordeliy, Valentin
PY - 2022
DA - 2022/04/28 00:00:00
PB - Springer Nature
SP - 440-450
IS - 5
VL - 29
SN - 1545-9993
SN - 1545-9985
ER -
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@article{2022_Borshchevskiy,
author = {Valentin Borshchevskiy and Kirill Kovalev and Ekaterina Round and Rouslan G. Efremov and Roman Astashkin and Gleb Bourenkov and Dmitry Bratanov and Taras Balandin and Igor Chizhov and Christian Baeken and Ivan Gushchin and Alexander Kuzmin and Alexey Alekseev and Andrey Rogachev and Dierk RAABE and MARTIN ENGELHARD and Ernst Bamberg and Georg Büldt and Valentin Gordeliy},
title = {True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins},
journal = {Nature Structural and Molecular Biology},
year = {2022},
volume = {29},
publisher = {Springer Nature},
month = {apr},
url = {https://doi.org/10.1038%2Fs41594-022-00762-2},
number = {5},
pages = {440--450},
doi = {10.1038/s41594-022-00762-2}
}
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Borshchevskiy, Valentin, et al. “True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins.” Nature Structural and Molecular Biology, vol. 29, no. 5, Apr. 2022, pp. 440-450. https://doi.org/10.1038%2Fs41594-022-00762-2.