Crystal structure of jumping spider rhodopsin-1 as a light sensitive GPCR

Proc Natl Acad Sci U S A. 2019 Jul 16;116(29):14547-14556. doi: 10.1073/pnas.1902192116. Epub 2019 Jun 27.


Light-sensitive G protein-coupled receptors (GPCRs)-rhodopsins-absorb photons to isomerize their covalently bound retinal, triggering conformational changes that result in downstream signaling cascades. Monostable rhodopsins release retinal upon isomerization as opposed to the retinal in bistable rhodopsins that "reisomerize" upon absorption of a second photon. Understanding the mechanistic differences between these light-sensitive GPCRs has been hindered by the scarcity of recombinant models of the latter. Here, we reveal the high-resolution crystal structure of a recombinant bistable rhodopsin, jumping spider rhodopsin-1, bound to the inverse agonist 9-cis retinal. We observe a water-mediated network around the ligand hinting toward the basis of their bistable nature. In contrast to bovine rhodopsin (monostable), the transmembrane bundle of jumping spider rhodopsin-1 as well that of the bistable squid rhodopsin adopts a more "activation-ready" conformation often observed in other nonphotosensitive class A GPCRs. These similarities suggest the role of jumping spider rhodopsin-1 as a potential model system in the study of the structure-function relationship of both photosensitive and nonphotosensitive class A GPCRs.

Keywords: G protein-coupled receptors; X-ray crystallography; bistability; retinal; rhodopsin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arthropod Proteins / isolation & purification
  • Arthropod Proteins / metabolism
  • Arthropod Proteins / ultrastructure*
  • Crystallography, X-Ray
  • HEK293 Cells
  • Humans
  • Ligands
  • Light
  • Molecular Dynamics Simulation
  • Protein Isoforms / isolation & purification
  • Protein Isoforms / metabolism
  • Protein Isoforms / ultrastructure
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Recombinant Proteins / ultrastructure
  • Rhodopsin / isolation & purification
  • Rhodopsin / metabolism
  • Rhodopsin / ultrastructure*
  • Signal Transduction / radiation effects*
  • Spiders*
  • Stereoisomerism
  • Structure-Activity Relationship


  • Arthropod Proteins
  • Ligands
  • Protein Isoforms
  • Recombinant Proteins
  • Rhodopsin

Associated data

  • PDB/6I9K