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Figure 2.
Figure 2. Stereo views of the tertiary structure of MPT51,
the structural superimposition with Ag85C2 and of the "active
site". (a) Secondary structure is color-coded: green, b-sheet;
cyan, a-helix; dark blue, 3[10] helix. The residues
corresponding to the catalytic triad in the Ag85 subunits are
shown as rods (yellow, carbon; blue, nitrogen; red, oxygen). (b)
Illustration of structural differences between MPT51 and Ag85C2.
Ribbon in light and dark blue corresponds to the active and
inhibitor-bound forms of Ag85C2. The b7-a9 loop and helix a9 of
MPT51 is shown in red, the fibronectin-binding loop in green.
(c) Electron density (s[A]-weighted 2F[o] -F[c] map, 30-1.7
Å, after automatic backbone tracing in ARP/wARP, contour
level 1.2s) of the active site of MPT51 with the catalytic triad
of Ag85C2 superimposed (rods in light blue). The final refined
model of MPT51 is shown with rods color-coded as in (a). The
Figure was prepared using RIBBONS.[53.]
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