Figure 3.
VAMP inhibitor (inh1) is shown in the middle panel in colored
secondary-structure boxes (loop, yellow; -strand,
cyan; helix, pink). On either side of the middle panel are the
enzyme residues (BoNT F–inh1). These interactions are equally
applicable for the common residues of inh1 and inh2 with minor
differences in distances, except for the interaction between
VAMP Asp40 and BoNT F Lys29, which is present only in inh2. The
color-coding for enzyme residues is based on their interaction
with the VAMP main chain (MC) or side chains (SC), and vice
versa. Colors for the VAMP–BoNT F interactions are: MC:SC,
pink; MC:MC, blue; SC:SC, cyan; SC:MC, brown. The intra-chain
interactions (in violet) of VAMP at exosite 1 have both MC:MC
and also hydrophobic SC:SC.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2009,
16,
789-794)
copyright 2009.
-strand,
cyan; helix, pink). On either side of the middle panel are the
enzyme residues (BoNT F–inh1). These interactions are equally
applicable for the common residues of inh1 and inh2 with minor
differences in distances, except for the interaction between
VAMP Asp40 and BoNT F Lys29, which is present only in inh2. The
color-coding for enzyme residues is based on their interaction
with the VAMP main chain (MC) or side chains (SC), and vice
versa. Colors for the VAMP–BoNT F interactions are: MC:SC,
pink; MC:MC, blue; SC:SC, cyan; SC:MC, brown. The intra-chain
interactions (in violet) of VAMP at exosite 1 have both MC:MC
and also hydrophobic SC:SC.