NDLI: Retinal counterion switch in the photoactivation of the G protein-coupled receptor rhodopsin

Content Provider	PubMed Central
Author	Yan, Elsa C. Y. Kazmi, Manija A. Ganim, Ziad Hou, Jian-min Pan, Douhai Chang, Belinda S. W. Sakmar, Thomas P. Mathies, Richard A.
Copyright Year	2003
Abstract	The biological function of Glu-181 in the photoactivation process of rhodopsin is explored through spectroscopic studies of site-specific mutants. Preresonance Raman vibrational spectra of the unphotolyzed E181Q mutant are nearly identical to spectra of the native pigment, supporting the view that Glu-181 is uncharged (protonated) in the dark state. The pH dependence of the absorption of the metarhodopsin I (Meta I)-like photoproduct of E181Q is investigated, revealing a dramatic shift of its Schiff base pKa compared with the native pigment. This result is most consistent with the assignment of Glu-181 as the primary counterion of the retinylidene protonated Schiff base in the Meta I state, implying that there is a counterion switch from Glu-113 in the dark state to Glu-181 in Meta I. We propose a model where the counterion switch occurs by transferring a proton from Glu-181 to Glu-113 through an H-bond network formed primarily with residues on extracellular loop II (EII). The resulting reorganization of EII is then coupled to movements of helix III through a conserved disulfide bond (Cys110–Cys187); this process may be a general element of G protein-coupled receptor activation.
Related Links	http://dx.doi.org/10.1073/pnas.1531970100
Ending Page	9267
Page Count	6
Starting Page	9262
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	16
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-08-05
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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