Nature Communications (Oct 2022)
Structural insights into light-driven anion pumping in cyanobacteria
- R. Astashkin,
- K. Kovalev,
- S. Bukhdruker,
- S. Vaganova,
- A. Kuzmin,
- A. Alekseev,
- T. Balandin,
- D. Zabelskii,
- I. Gushchin,
- A. Royant,
- D. Volkov,
- G. Bourenkov,
- E. Koonin,
- M. Engelhard,
- E. Bamberg,
- V. Gordeliy
Affiliations
- R. Astashkin
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)
- K. Kovalev
- European Molecular Biology Laboratory, Hamburg unit c/o DESY
- S. Bukhdruker
- European Synchrotron Radiation Facility Grenoble
- S. Vaganova
- Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich
- A. Kuzmin
- Research Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow Institute of Physics and Technology
- A. Alekseev
- Research Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow Institute of Physics and Technology
- T. Balandin
- Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich
- D. Zabelskii
- European XFEL GmbH
- I. Gushchin
- Research Center for Molecular Mechanisms of Aging and Age-related Diseases, Moscow Institute of Physics and Technology
- A. Royant
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)
- D. Volkov
- Institute of Biological Information Processing (IBI-7: Structural Biochemistry), Forschungszentrum Jülich
- G. Bourenkov
- European Molecular Biology Laboratory, Hamburg unit c/o DESY
- E. Koonin
- National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health
- M. Engelhard
- Department Structural Biochemistry, Max Planck Institute of Molecular Physiology
- E. Bamberg
- Max Planck Institute of Biophysics
- V. Gordeliy
- Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)
- DOI
- https://doi.org/10.1038/s41467-022-34019-9
- Journal volume & issue
-
Vol. 13,
no. 1
pp. 1 – 13
Abstract
Here, the authors present four high-resolution structures of SyHR protein from cyanobacterial anion pumps family: chloride and sulfate bound forms and two active state structures. These structures provide insights into the molecular mechanisms of SyHR and cyanobacterial anion pumps in general.
