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Area of Science:

  • Structural Biology
  • Microbial Biochemistry
  • Membrane Proteins

Background:

  • Heliorhodopsins (HeRs) are a recently discovered family of microbial rhodopsins found across diverse life forms.
  • Despite sharing key features with other rhodopsins, HeRs exhibit low sequence identity and a reversed membrane orientation.
  • Limited structural and mechanistic information hindered understanding of HeR function and evolution.

Purpose of the Study:

  • To determine the high-resolution structure of Heliorhodopsin from an uncultured archaeon.
  • To elucidate the structural similarities and differences between HeRs and other microbial rhodopsins.
  • To investigate the photoactivation mechanism and functional implications of HeR structure.

Main Methods:

  • X-ray crystallography to determine the 2.4-Å resolution structure of HeR.
  • Structural analysis to compare HeR with known rhodopsin families.
  • Biophysical analyses to probe functional aspects of the determined structure.

Main Results:

  • The overall fold of HeR is similar to bacteriorhodopsin, but with significant divergence in the retinal-binding pocket residues.
  • HeR possesses a unique lateral fenestration above the retinal β-ionone ring, crucial for environmental retinal capture.
  • Hydrophobic residues in the extracellular half likely prevent proton and ion permeation.

Conclusions:

  • The determined HeR structure provides critical insights into the structural diversity of microbial rhodopsins.
  • The unique structural features, including the lateral fenestration, highlight novel functional adaptations in HeRs.
  • This study advances the understanding of HeR function and their evolutionary relationship within the rhodopsin superfamily.