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TitleCryo-EM structure of a nanobody-bound heliorhodopsin.
Journal, issue, pagesBiochem Biophys Res Commun, Vol. 750, Page 151398, Year 2025
Publish dateMar 1, 2025
AuthorsRuixue Xia / Mingxia Sun / Yang Lu / Na Wang / Anqi Zhang / Changyou Guo / Zhenmei Xu / Xuehui Cai / Yuanzheng He /
PubMed AbstractHeliorhodopsins (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 ...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.
External linksBiochem Biophys Res Commun / PubMed:39889627
MethodsEM (single particle)
Resolution3.23 Å
Structure data

63157

9ljj

EMDB-63157, PDB-9ljj:
cryo-EM structure of a nanobody bound heliorhodopsin
Method: EM (single particle) / Resolution: 3.23 Å

Chemicals

ChemComp-RET:
RETINAL

ChemComp-ACT:
ACETATE ION

ChemComp-PX2:
1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE

ChemComp-PLM:
PALMITIC ACID

Source
  • escherichia coli (E. coli)
  • vicugna pacos (alpaca)
KeywordsMEMBRANE PROTEIN / bacterial rhodopsin

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