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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].
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