Figure 3 - full size


Figure 3.
Figure 3. Structural Features of CTPR2/3(A) Representation of the electron density of CTPR2 in the vicinity of Tyr23(B2) and Tyr24(B2). A 2F[o] - F[c] map (blue), contoured at 1 s, is displayed over a stick model of the structure to demonstrate the quality of the data.(B-D) Representation of the overall folds of (B) CTPR2 and (C) CTPR3 and (D) a stereo view of the overlaid structures of CTPR2 (red) and CTPR3 (blue). They are represented by a tubular worm that snakes through their C^a backbones. CTPR2 (red) corresponds to 86 amino acids from Gly3 to Gly15(solvating helix), and CTPR3 (blue) corresponds to 119 amino acids from Asn2 to Gly15(solvating helix). The N and C termini are marked on each diagram.(E) An illustration showing the two IPTG molecules (space fill, purple and blue) that induce a dimer interface between two molecules of CTPR3 (rendered as a cyan and red C^a trace). The side chains of residues that interact with the IPTG are rendered as sticks, with the chloride ion caught between the two IPTG molecules rendered as green space fills. (A)-(E) were produced with SPOCK [53].

The above figure is reprinted by permission from Cell Press: Structure (2003, 11, 497-508) copyright 2003.