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Figure 2.
Figure 2 Molecular surface representation. (A, B) Secondary
structure assignments along the colicin D (A) and ImmD (B)
sequences. Residues involved in complex formation are
highlighted in bold. (C) The binary colicin D (yellow) -ImmD
(green) complex. The orientation is the same as in Figure 1A.
The red-coloured region corresponds to ImmD positions located
outside the interface, but whose mutation abolishes or reduces
the inhibitory capacity. (D) Surface mapping of the colicin D
catalytic active site residues. Unmutated positions are coloured
grey. Residues whose mutation does not alter tRNase activity are
shown in green, those whose substitution results in partially or
fully inactivated proteins are depicted in orange and red,
respectively. For clarity, only residues whose mutation results
in complete loss of activity are labelled. (E) ImmD
foot-printing (green) at the colicin D surface. The His611
residue is coloured yellow. The orientation is the same as in
(D). (F) Open leaflet representation of the complex illustrating
the electrostatic complementarity between colicin D and ImmD.
Regions of the surface with negative potential are coloured red
and those with positive potential are in blue. The colicin D
orientation is similar as in (D). The ImmD is rotated 180°
around the vertical axis. (G) Surface mapping of the ImmD
residues involved in the inhibitory effect. Colour coding is the
same as in (D). The orientations of the ImmD in the top and
bottom panels are related by a 180° rotation around the vertical
axis.
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