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Figure 3.
Fig. 3. Superposition of the maltohexaose (sticks) and
maltononaose (lines) inhibitor structures. At subsite +3 the
conformation of the maltohexaose inhibitor is more bent toward
Phe^196 and is stabilized by Lys47, which is Arg47 in the CGTase
from B. circulans strain 251. Moreover, the replacement of Tyr89
(B. circulans CGTase) by Asp89 (T. thermosulfurigenes EM1
CGTase) makes that the "straight" maltononaose conformation at
subsite +3 is not as stably bound^ in T. thermosulfurigenes EM1
CGTase than as in B. circulans CGTase.
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