1L9H: Crystal Structure Of Bovine Rhodopsin At 2.6 Angstroms Resolution

Citation:
Abstract
Activation of G protein-coupled receptors (GPCRs) is triggered and regulated by structural rearrangement of the transmembrane heptahelical bundle containing a number of highly conserved residues. In rhodopsin, a prototypical GPCR, the helical bundle accommodates an intrinsic inverse-agonist 11-cis-retinal, which undergoes photo-isomerization to the all-trans form upon light absorption. Such a trigger by the chromophore corresponds to binding of a diffusible ligand to other GPCRs. Here we have explored the functional role of water molecules in the transmembrane region of bovine rhodopsin by using x-ray diffraction to 2.6 A. The structural model suggests that water molecules, which were observed in the vicinity of highly conserved residues and in the retinal pocket, regulate the activity of rhodopsin-like GPCRs and spectral tuning in visual pigments, respectively. To confirm the physiological relevance of the structural findings, we conducted single-crystal microspectrophotometry on rhodopsin packed in our three-dimensional crystals and show that its spectroscopic properties are similar to those previously found by using bovine rhodopsin in suspension or membrane environment.
PDB ID: 1L9HDownload
MMDB ID: 104407
PDB Deposition Date: 2002/3/23
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
Similar Structures:
Biological Unit for 1L9H: monomeric; determined by author
Molecular Components in 1L9H
Label Count Molecule
Protein (1 molecule)
1
Rhodopsin(Gene symbol: RHO)
Molecule annotation
Chemicals (24 molecules)
1
2
2
6
3
3
4
4
5
4
6
4
7
1
* Click molecule labels to explore molecular sequence information.

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