High-resolution structural studies of the retinal--Glu113 interaction in rhodopsin.
The key to understanding the reaction mechanism of rhodopsin lies in determining the structure of the retinal binding site and in defining the charge interactions between Glu113 and the retinal protonated Schiff base chromophore. We have been using 13C-NMR chemical shift data to determine the location of the Glu113 carboxyl side chain in relation to the retinal. The NMR data constrain one of the carboxylate oxygens of Glu113 to be ca. 3 A from the C12 position of the retinal with the second oxygen oriented away from the conjugated chain. A water molecule forming a hydrogen bond with the Schiff base is incorporated into the model to account for the high C = N stretching frequency [Han et al., Biophys. J., 65 (1993) 899]. In this study, we have refined the counterion position and have shown that it can reproduce the observed chemical shift data as well as the red-shifted absorption maximum of rhodopsin. Furthermore, the retinal binding site geometry derived from the NMR constraints can be readily incorporated into a recent structural model of the apoprotein.
Han
M
M
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA.
Smith
S O
SO
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D018698:Glutamic Acid; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D012172:Retinaldehyde / Q000737:chemistry / Q000378:metabolism*; D012243:Rhodopsin / Q000737:chemistry* / Q000378:metabolism*; D012545:Schiff Bases; D014714:Vertebrates
D012545:Schiff Bases; D018698:Glutamic Acid; D012243:Rhodopsin; D012172:Retinaldehyde