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8QLE

Crystal structure of the light-driven sodium pump ErNaR in the monomeric form at pH 4.6

Summary for 8QLE
Entry DOI10.2210/pdb8qle/pdb
DescriptorBacteriorhodopsin-like protein, EICOSANE, OLEIC ACID, ... (4 entities in total)
Functional Keywordsretinal, ion transport, rhodopsin, photocycle, sodium transport, membrane protein
Biological sourceErythrobacter
Total number of polymer chains1
Total formula weight35973.53
Authors
Kovalev, K.,Podoliak, E.,Lamm, G.H.U.,Astashkin, R.,Bourenkov, G. (deposition date: 2023-09-19, release date: 2024-04-24)
Primary citationPodoliak, E.,Lamm, G.H.U.,Marin, E.,Schellbach, A.V.,Fedotov, D.A.,Stetsenko, A.,Asido, M.,Maliar, N.,Bourenkov, G.,Balandin, T.,Baeken, C.,Astashkin, R.,Schneider, T.R.,Bateman, A.,Wachtveitl, J.,Schapiro, I.,Busskamp, V.,Guskov, A.,Gordeliy, V.,Alekseev, A.,Kovalev, K.
A subgroup of light-driven sodium pumps with an additional Schiff base counterion.
Nat Commun, 15:3119-3119, 2024
Cited by
PubMed 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.
PubMed: 38600129
DOI: 10.1038/s41467-024-47469-0
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

227111

数据于2024-11-06公开中

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