Figure 3.
FIGURE 3. Mesotrypsin conformational changes upon BPTI
binding. A, superposition of the mesotrypsin-BPTI complex
(mesotrypsin in orange and BPTI in blue/cyan) with the
mesotrypsin-benzamidine complex (mesotrypsin in beige and
benzamidine in red) highlights several differences induced by
BPTI binding. Significant movements in the positions of side
chains, illustrated by the black arrows, include the upward
displacement of Arg-193 by 6 Å displacing a
water molecule, adoption of an alternate rotamer by His-40, and
displacement of Asp-153 by 1 Å to enable formation of a
water-bridged ionic interaction with Arg-193. B, environment
surrounding the BPTI-bound position of mesotrypsin Arg-193 is
shown with 2F[o]-F[c] map contoured at 1.5 sigma. Arg-193 forms
direct H-bonds to the carbonyl oxygens of Trp-141 and Pro-152,
and water bridged interactions with the side chains of Asp-153
and BPTI Arg-17.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2007,
283,
4115-4123)
copyright 2007.
6 Å displacing a
water molecule, adoption of an alternate rotamer by His-40, and
displacement of Asp-153 by 1 Å to enable formation of a
water-bridged ionic interaction with Arg-193. B, environment
surrounding the BPTI-bound position of mesotrypsin Arg-193 is
shown with 2F[o]-F[c] map contoured at 1.5 sigma. Arg-193 forms
direct H-bonds to the carbonyl oxygens of Trp-141 and Pro-152,
and water bridged interactions with the side chains of Asp-153
and BPTI Arg-17.