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Figure 5.
Figure 5. Structures of Bb^C428-C435 Inhibitor Complexes(A)
Superposition of the active sites of Bb^C428-C435 (gold) and
Bb^C428-C435-BCX583 (light green) crystal structures. The
inhibitor (BCX583) covalently linked to Ser^195 is held in
position by hydrogen bonding to Asp^715(226) through a water
molecule (lavender). The L2 loop (red) is seen only in the
inhibitor complex structure.(B) Comparison of the active sites
of Bb^C428-C435-DIP and Bb^C428-C435. The backbone of the
inhibitor-bound Bb^C428-C435 is shown in light green color,
while the inhibitor-free Bb^C428-C435 is shown in gold color.
Covalently bound DIP molecule points its phosphoryl oxygen into
the putative oxyanion hole (marked with black star) and forces
it to acquire a tight β turn from a zymogen-like 3[10] helix
(transparent red color) conformation.(C) Stereo close-up of the
superposition of the 670(191)-674(194) segment of Bb^C428-C435
(gold) and Bb^C428-C435-DIP complex (light green). The
orientational difference of carbonyl oxygen of the residue
671(192) is indicated in the boxed area.
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