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Figure 2.
Fig. 2. A, stereo drawing of Sigma A-weighted 2 mF[o]
 DF[c] maps
(20) contoured at 1  around the
 A169L/ C170W
mutation site showing the good definition of the two new side
chains and the reorientation of both gating residues tyrosine
Tyr279 and
phenylalanine Phe^280. The
figure was prepared using BOBSCRIPT (24) and RASTER3D (25, 26).
B, stereo view of the superposition of the COMM domains of
wild-type TRPSIPP and A169L/ C170WF-IPP.
Mutated and gating residues of the -subunit are
shown in a ball-and-stick representation. C  trace and
residues of wild-type TRPSIPP are red ( -subunit),
dark blue, ( -subunit),
and yellow (COMM domain, the double mutant is green, carbon
atoms of the -ligands
and the cofactor PLP are gray, oxygen atoms red, nitrogen atoms
blue, and phosphate is magenta. Panels A and B are related by an
~90° rotation around the axis perpendicular to the paper
plane. The figure was prepared using MOLSCRIPT (27) and RASTER3D
(25, 26).
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