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. 2010 Feb 8;16(6):1744-9.
doi: 10.1002/chem.200903194.

Photochemistry of visual pigment in a G(q) protein-coupled receptor (GPCR)--insights from structural and spectral tuning studies on squid rhodopsin

Sivakumar Sekharan  1 , Ahmet Altun, Keiji Morokuma
Affiliations

Photochemistry of visual pigment in a G(q) protein-coupled receptor (GPCR)--insights from structural and spectral tuning studies on squid rhodopsin

Sivakumar Sekharan et al. Chemistry. .
No abstract available

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Figures

Figure 1
Figure 1
Side and top view of the overlay of the backbone atom positions of seven transmembrane α-helices of 2.5 Å (green), 3.7 Å (blue) crystal structures and QM/MM optimized structure (red) of the WS2 model of squid rhodopsin.
Figure 2
Figure 2
Optimized QM/MM model (WS2) of squid rhodopsin containing two internal water molecules (W1, W2). The H-bond network between SB nitrogen of PSBR chromophore (cyan), and side chain oxygen of Asn87 (magenta), Tyr111 (green), Glu180 (yellow) are shown in black dots. The distances in numbers are given in Table 1.
Figure 3
Figure 3
Comparison of the bond length alternation (bottom), bond angles (middle) and dihedral angles (top) along the conjugated carbon chain of the 2.5 Å (red), 3.7 Å (green) X-ray and QM/MM retinal geometry in four different set-ups; WS0 (blue), WS1 (cyan), WS2 (black), WS3 (magenta). The experimental structure sets taken from chain A. The dihedral angle deviations are from either cis (0°) or the trans (180°) configuration.
Figure 4
Figure 4
Overlay of the 11-cis-retinal protonated Schiff base (PSBR) and Glu180, Tyr111, Asn87, residues of 2.5 Å (green), 3.7 Å (blue) crystal structures and QM/MM optimized structure (red) of the WS2 model of squid rhodopsin.
See this image and copyright information in PMC

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