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![[Figure 3]](gm5099fig3mag.jpg)
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Figure 3
Comparison of the main channel and heme cavity of wild-type CATPO (a) and its E484A (b), T188A (c) and T188F (d) variants. The corresponding omit maps for residues, ligands and waters are shown for the four cases at 1.0 r.m.s.d. The gate residues Glu484 and Thr188 are located at the top of each figure at the entry to the main channel. Also shown are the conserved residues lining the channel and the heme cavity: His82, Val123, Asp135, Phe160, Phe161, Phe168 and Tyr369. The ring of hydrophobic residues that includes Val123 defines the narrowest point of the main channel. Heme d is found in wild-type CATPO (a) and the T188A variant (c), whereas heme b is found in the E484A (b) and T188F (d) variants. Changes in solvent organization are evident in the structures. The water molecules of the recombinant wild-type enzyme and their equivalents in the variants are labelled numerically: W1–W11. The water molecule WX in the E484A variant does not correspond to any water in recombinant wild-type CATPO. The insets show the difference in the side-chain geometry of the mutated and nonmutated residues. |
![[Figure 3]](gm5099fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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