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Cryo-EM structure of a nanobody-bound heliorhodopsin. | LitMetric

Cryo-EM structure of a nanobody-bound heliorhodopsin.

Biochem Biophys Res Commun

HIT Center for Life Sciences, School of Life Science and Technology, Faculty of Life Sciences and Medicine, Harbin Institute of Technology, Harbin, 150001, China; Frontiers Science Center for Matter Behave in Space Environment, Harbin Institute of Technology, Harbin, 150001, China. Electronic address:

Published: March 2025

Heliorhodopsins (HeRs) represent a distinct class of microbial rhodopsins (MRs) with an inverted membrane topology compared to other MRs. Previous structural studies have shown that HeRs lack a proton acceptor residue, and protons are never released from the protein. In this study, we present the cryo-electron microscopy (cryo-EM) structure of HeR bound to a nanobody. The structure reveals an acetate-like molecule in the Schiff base cavity (SBC) on the intracellular side of HeR under neutral condition. Structural comparisons and analyses suggest that the acetate molecule may function as a proton acceptor for the protonated retinal Schiff base (RSB) and act as a mediator for the intramolecular signaling transduction in HeR during light stimulation. These structural insights shed new light on the mechanism and function of HeR.

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Source
http://dx.doi.org/10.1016/j.bbrc.2025.151398DOI Listing

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