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Figure 2.
Figure 2. Solution structure of the P. equi dockerin. a,
Stereo view of the ensemble of 34 structures, colored from red
at the N-terminus to blue at the C-terminus. b, Stereo
MOLSCRIPT27 diagram of the dockerin structure, showing the
locations of disulfide bridges and the binding site residues
discussed in the text. The protein present in the sample
consisted of 52 residues -- that is, the 38-residue 'core'
sequence that is highly conserved in fungal dockerins, plus all
12 residues C-terminal of the core sequence prior to the start
of the second dockerin domain, and two N-terminal residues from
the GST-tag. The figure shows only the ordered residues -2 -44.
c, Surface of the protein, in the same orientation as (b). Side
chains of residues Tyr 8 and Trp 35 are in purple, and Asp 23 in
light lilac. Acidic residues are in red, basic in dark blue and
hydrophobic in yellow.
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