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PMID: 16908857 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Local peptide movement in the photoreaction intermediate of rhodopsin.

Nakamichi H, Okada T

Abstract

Photoactivation of the visual rhodopsin, a prototypical G protein-coupled receptor (GPCR), involves efficient conversion of the intrinsic inverse-agonist 11-cis-retinal to the all-trans agonist. This event leads to the rearrangement of the heptahelical transmembrane bundle, which is thought to be shared by hundreds of GPCRs. To examine this activation mechanism, we determined the x-ray crystallographic model of the photoreaction intermediate of rhodopsin, lumirhodopsin, which represents the conformational state having the nearly complete all-trans agonist form of the retinal. A difference electron density map clearly indicated that the distorted all-trans-retinal in the precedent intermediate bathorhodopsin relaxes by dislocation of the beta-ionone ring in lumirhodopsin, along with significant peptide displacement in the middle of helix III, including approximately two helical turns. This local movement results in the breaking of the electrostatic interhelical restraints mediated by many of the conserved residues among rhodopsin-like GPCRs, with consequent acquisition of full activity.

MeSH Terms
Animals Cattle Crystallography, X-Ray Models, Molecular Peptides/chemistry,metabolism Photochemistry Protein Structure, Tertiary Rhodopsin/chemistry,metabolism Spectrum Analysis Static Electricity
Chemicals
Peptides Rhodopsin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Nakamichi Hitoshi
Biological Information Research Center, National Institute of Advanced Industrial Science and Technology, Tokyo 135-0064, Japan.
Okada Tetsuji
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
2006-08-22
Epub
2006-00-14
Pages
12729-34
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC1562544
Subset
IM
Databases
PDB
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