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Figure 6
XF-MS probes bound water mediated signal transfer pathway in bovine rhodopsin. (a) DR-plots of dark (black) versus meta II (red) for the peptide p333–348 (at the solvent exposed cytoplasmic side) and p160–164 (at the TM region) for modified residues as indicated. (b) Pictorial summary of relative solvent accessibility changes for the photoactivation of dark to meta II state. Residues with rate constants >0.1 s−1 are shown as sticks. The color coding represents the ratio of rate constants between meta II and rhodopsin. Conserved transmembrane waters are shown as cyan spheres. The changes in rates of modification reflect local structural changes inside the TM domain upon formation of meta II. The results demonstrate disruption and reorganization of multiple close-packing interactions, mediated by both side chains and bound waters. The information is transmitted from the chromophore (ligand-binding site) to the cytoplasmic surface for G-protein activation. Results from Angel, Gupta et al. (2009BB2).

Journal logoJOURNAL OF
SYNCHROTRON
RADIATION
ISSN: 1600-5775
Volume 23| Part 5| September 2016| Pages 1056-1069
https://doi.org/10.1107/S1600577516009024
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