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Figure 2.
FIGURE 2. The three-dimensional structures of the C.
cellulolyticum cohesin-dockerin complexes. a depicts the
structure of Coh-DocA16S/L17T with the dockerin color-ramped
from N terminus (blue) to C terminus (red) and the cohesin in
pale brown. In this complex the hydrophobic residues Phe-48 and
Ala-47 dominate the hydrophobic contribution of the dockerin,
and these residues are shown as ball-and-stick. Ca^2+ ions are
shown as shaded spheres. b shows the CohDocA47S/F48T complex,
similarly colored. Here Leu-17 and Ala-16 of the dockerin form
the basis of the hydrophobic surface of the dockerin. c depicts
an overlap of the two binding modes showing the very high degree
of overall similarity reflecting the internal 2-fold symmetry of
the dockerin itself (see text). A47S/F48T is shown in blue and
A16S/L17T in yellow.
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