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Figure 6.
Figure 6. Comparison of the g moiety recognition site. (a)
A space-filling stereo drawing of the active site of Tf-IPMDH,
viewed from the right-hand side of Figure 7b. The substrate is
shown in ball-and-stick representation. Atoms are color-coded:
oxygen, red; nitrogen, blue; and carbon, gray. A green ball
represents a sulfur atom of a methionine residue and a small
magenta ball indicates the magnesium ion. The carbon atoms in
the hydrophobic pocket are highlighted in orange. Residues
forming the hydrophobic pocket are labeled with their residue
numbers. Schematic representations of the active site of (b)
Tf-IPMDH (closed conformation), (c) Ec-ICDH (closed
conformation), (d) St-IPMDH (closed conformation), (e) Tt-IPMDH
IPM complex (open conformation). The orientation is as in (a).
(d) Was generated by the superposition of IPM and Mg of the
Tf-IPMDH binary complex onto the structure of St-IPMDH solved
without IPM and Mg. The protein backbone is shown in a ribbon
representation. The substrate molecules and sidechains lying in
the active sites are shown in ball-and-stick representation. The
color coding of the atoms is as in (a). Residues interacting
with the g moiety of the substrates are labeled with their
residue numbers. The figures were generated with MOLSCRIPT [36]
and RASTER3D [37].
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