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 and V. Gordeliy ()
Additional contact information
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: 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)

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: Abstract Transmembrane ion transport is a key process in living cells. Active transport of ions is carried out by various ion transporters including microbial rhodopsins (MRs). MRs perform diverse functions such as active and passive ion transport, photo-sensing, and others. In particular, MRs can pump various monovalent ions like Na+, K+, Cl−, I−, NO3−. The only characterized MR proposed to pump sulfate in addition to halides belongs to the cyanobacterium Synechocystis sp. PCC 7509 and is named Synechocystis halorhodopsin (SyHR). The structural study of SyHR may help to understand what makes an MR pump divalent ions. Here we present the crystal structure of SyHR in the ground state, the structure of its sulfate-bound form as well as two photoreaction intermediates, the K and O states. These data reveal the molecular origin of the unique properties of the protein (exceptionally strong chloride binding and proposed pumping of divalent anions) and sheds light on the mechanism of anion release and uptake in cyanobacterial halorhodopsins. The unique properties of SyHR highlight its potential as an optogenetics tool and may help engineer different types of anion pumps with applications in optogenetics.

Date: 2022
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-022-34019-9 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34019-9

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-022-34019-9

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().