A subgroup of light-driven sodium pumps with an additional Schiff base counterion

E. Podoliak, G. H. U. Lamm, E. Marin, A. V. Schellbach, D. A. Fedotov, A. Stetsenko, M. Asido, N. Maliar, G. Bourenkov, T. Balandin, C. Baeken, R. Astashkin, T. R. Schneider, A. Bateman, J. Wachtveitl, I. Schapiro, V. Busskamp, A. Guskov, V. Gordeliy, A. Alekseev () and K. Kovalev ()
Additional contact information
E. Podoliak: University Hospital Bonn, Medical Faculty
G. H. U. Lamm: Goethe University Frankfurt
E. Marin: University of Groningen
A. V. Schellbach: Goethe University Frankfurt
D. A. Fedotov: The Hebrew University of Jerusalem
A. Stetsenko: University of Groningen
M. Asido: Goethe University Frankfurt
N. Maliar: University of Cambridge
G. Bourenkov: EMBL Hamburg c/o DESY
T. Balandin: Forschungszentrum Jülich
C. Baeken: Forschungszentrum Jülich
R. Astashkin: Institut de Biologie Structurale (IBS)
T. R. Schneider: EMBL Hamburg c/o DESY
A. Bateman: Wellcome Genome Campus
J. Wachtveitl: Goethe University Frankfurt
I. Schapiro: The Hebrew University of Jerusalem
V. Busskamp: University Hospital Bonn, Medical Faculty
A. Guskov: University of Groningen
V. Gordeliy: Forschungszentrum Jülich
A. Alekseev: Institute for Auditory Neuroscience and InnerEarLab
K. Kovalev: EMBL Hamburg c/o DESY

Nature Communications, 2024, vol. 15, issue 1, 1-16

Abstract: Abstract Light-driven sodium pumps (NaRs) are unique ion-transporting microbial rhodopsins. The major group of NaRs is characterized by an NDQ motif and has two aspartic acid residues in the central region essential for sodium transport. Here we identify a subgroup of the NDQ rhodopsins bearing an additional glutamic acid residue in the close vicinity to the retinal Schiff base. We thoroughly characterize a member of this subgroup, namely the protein ErNaR from Erythrobacter sp. HL-111 and show that the additional glutamic acid results in almost complete loss of pH sensitivity for sodium-pumping activity, which is in contrast to previously studied NaRs. ErNaR is capable of transporting sodium efficiently even at acidic pH levels. X-ray crystallography and single particle cryo-electron microscopy reveal that the additional glutamic acid residue mediates the connection between the other two Schiff base counterions and strongly interacts with the aspartic acid of the characteristic NDQ motif. Hence, it reduces its pKa. Our findings shed light on a subgroup of NaRs and might serve as a basis for their rational optimization for optogenetics.

Date: 2024
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DOI: 10.1038/s41467-024-47469-0

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