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Figure 4.
Fig. 4. Comparison of the side chain packing around the
mutation sites in the quintuple mutant and the corresponding
regions in the wild-type PA c[551] and HT c[552]. Amino acids
mentioned throughout are designated with a one-letter code.
Residues in HT c[552] are shown with the numbering used for
those in PA c[551]. The mutated side chains of the quintuple
mutant and the corresponding ones of the wild-type PA c[551] and
HT c[552] are colored purple, green, and red, respectively. A,
the hydrophobic region around Phe-7 and Val-13 of the wild-type
PA c[551] and the corresponding regions in the quintuple mutant
and HT c[552]. B, the loop and half of the third helix region
from Phe-34 to Leu-44 of the wild-type PA c[551] and the
corresponding regions in the quintuple mutant and HT c[552]. C,
the internal hydrophobic region around Val-78 and the heme of
the wild type and the corresponding regions in the quintuple
mutant and HT c[552].
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