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Figure 3.
Figure 3. The C terminus of hBH. Residues 447–454 of the
wild-type protein, as well as the catalytic Cys73, are shown as
bonds colored according to atom type. The corresponding residues
of the Cys73→Ser/ΔGlu455 mutant protein are shown in cyan.
The sidechains of the catalytic residues His372 and Asp396 are
shown with yellow bonds, as is the sidechain of Gln67, which
stabilizes the oxyanion intermediate during catalysis.
Hydrogen-bond interactions of the mutant protein – between the
C-terminal alanine and the sidechain of Gln67 and the amide
nitrogen atoms of Ser73 and Trp74, and between Ser73 and the
backbone amide of residue 373 – are shown as dotted white
lines. Arrows indicate the Cα atoms of labeled residues. Gly451
is the elbow at which the C-terminal arm rotates and extends.
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