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. Author manuscript; available in PMC: 2014 Jun 5.
Published in final edited form as: Science. 2012 Dec 7;338(6112):1340–1343. doi: 10.1126/science.1226135

Figure 2.

Figure 2

A. Crystal structure of Q108K:K40L:T51V:T53C:Y19W: R58W:T29L hCRBPII with Thr1, Gln4, Asp91, and Ile110 highlighted to show hydrogen bonding to W1, extending to the iminium nitrogen. B. The overlay of the crystal structures of Q108K:K40L:T51V:T53C:Y19W:R58W :T29L hCRBPII (591 nm, cyan structure) and Q108K:K40L: T51V:T53C:Y19W:R58W:T29L:Q4R hCRBPII (622 nm, yellow structure) indicating the lack of an ordered water molecule with the Q4R mutant that leads to further bathochromic shift of the retinylidene protein complex. As exemplified in the latter two structures, all mutants that have an ordered water molecule adopt the cis-imine geometry. Conversely, trans-imine geometry is observed in all Q4 mutants without the ordered water molecule (fig. S7). C. Crystal structure of Q108K:K40L:T51V:T53C:Y19W: R58W:T29L hCRBPII (591 nm) illustrates the opening near Ala33. D. Crystal structure of Q108K:K40L:T51V:T53C:Y19W:R58W:T29L:A33W hCRBPII (606 nm) shows substantial closing of the orifice (A33W surface shown in red).