Crystal structure of squid rhodopsin

@article{Murakami2008CrystalSO,
  title={Crystal structure of squid rhodopsin},
  author={Midori Murakami and Tsutomu Kouyama},
  journal={Nature},
  year={2008},
  volume={453},
  pages={363-367}
}
Invertebrate phototransduction uses an inositol-1,4,5-trisphosphate signalling cascade in which photoactivated rhodopsin stimulates a Gq-type G protein, that is, a class of G protein that stimulates membrane-bound phospholipase Cβ. The same cascade is used by many G-protein-coupled receptors, indicating that invertebrate rhodopsin is a prototypical member. Here we report the crystal structure of squid (Todarodes pacificus) rhodopsin at 2.5 Å resolution. Among seven transmembrane α-helices… 

Crystallographic analysis of the primary photochemical reaction of squid rhodopsin.

Dynamics of the internal water molecules in squid rhodopsin.

A G protein-coupled receptor at work: the rhodopsin model.

Comparative Analysis of GPCR Crystal Structures †

TLDR
To fully understand the structural and functional aspects of rhodopsin it is necessary to critically examine crystal structures of its different photointermediates.

Recent advances in biophysical studies of rhodopsins - Oligomerization, folding, and structure.

  • L. BrownO. Ernst
  • Biology, Chemistry
    Biochimica et biophysica acta. Proteins and proteomics
  • 2017

Structural divergence and functional versatility of the rhodopsin superfamily.

  • T. KouyamaM. Murakami
  • Biology
    Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology
  • 2010
TLDR
Comparison of high-resolution crystal structures for ten members of the rhodopsin superfamily provides a hint to elucidate the common structural motif that is utilized to stabilize their tertiary structures as well as unique architectures that are relevant to specific functions.

Functional analysis of the second extracellular loop of rhodopsin by characterizing split variants.

TLDR
The results suggest that ECL2 'mechanically' drives the conformational change of rhodopsin.

Structural elements of the signal propagation pathway in squid rhodopsin and bovine rhodopsin.

TLDR
Differences in the hydrogen bond network may play significant functional roles in the signal propagation from the retinal binding site to the cytoplasmic site, including transmembrane helix (TM) 6 to which the G-protein binds.

Crystal structure of opsin in its G-protein-interacting conformation

TLDR
The 3.2 Å crystal structure of the bovine Ops*–GαCT peptide complex is presented and signal transfer from the receptor to the G protein nucleotide-binding site is discussed.
...

References

SHOWING 1-10 OF 52 REFERENCES

Crystal structure of rhodopsin: a G-protein-coupled receptor.

Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) respond to a variety of different external stimuli and activate G proteins. GPCRs share many structural

Crystallization and crystal properties of squid rhodopsin.

TLDR
Preliminary crystallographic analysis, together with linear dichroism results, suggested that the rhodopsin dimers are packed in such a manner that their transmembrane helices are aligned nearly parallel to the c axis.

Three-dimensional structure of an invertebrate rhodopsin and basis for ordered alignment in the photoreceptor membrane.

TLDR
A three-dimensional structure of squid rhodopsin determined by cryo-electron microscopy of two-dimensional crystals is presented, providing the first indication of the structural basis for rhodopod alignment in the microvillar membrane.

A Purified Agonist-Activated G-Protein Coupled Receptor: Truncated Octopus Acid Metarhodopsin

TLDR
This paper reports the large scale preparation of a stable, homogenous species, truncated octopus rhodopsin (t-rhodopin) in which proteolysis has removed the proline-rich C-terminal and this species retains the spectral properties and the ability for light-induced G-protein activation of unproteolyzedOctopus r Rhodopsin.

High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor.

TLDR
Although the location of carazolol in the beta2-adrenergic receptor is very similar to that of retinal in rhodopsin, structural differences in the ligand-binding site and other regions highlight the challenges in using rhodopin as a template model for this large receptor family.

An Activation Switch in the Rhodopsin Family of G Protein-coupled Receptors

TLDR
This work has identified residue Asn-7.49, of the NPxxY motif of TM 7, as a molecular switch in the mechanism of thyrotropin receptor (TSHr) activation, and focused on the transmembrane region and in particular on a network of polar interactions between highly conserved residues.

High-Resolution Crystal Structure of an Engineered Human β2-Adrenergic G Protein–Coupled Receptor

TLDR
Although the location of carazolol in the β2-adrenergic receptor is very similar to that of retinal in rhodopsin, structural differences in the ligand-binding site and other regions highlight the challenges in using rhodopin as a template model for this large receptor family.

Direct observation of the complex formation of GDP-bound transducin with the rhodopsin intermediate having a visible absorption maximum in rod outer segment membranes.

TLDR
The results strongly suggest that the protein conformational change of the rhodopsin intermediate after binding to Gt is important for the induction of the nucleotide release from the alpha-subunit of Gt.

Crystal structure of the human β2 adrenergic G-protein-coupled receptor

TLDR
The β2AR structure differs from rhodopsin in having weaker interactions between the cytoplasmic ends of transmembrane (TM)3 and TM6, involving the conserved E/DRY sequences, which may be responsible for the relatively high basal activity and structural instability of the β2 AR.
...