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Figure 1.
Fig. 1. Overall structure of InlA/hEC1 (dark/light blue).
(A) Reengineered residues are indicated by spheres. Although
separated by 34 Å, combinations of substitutions from
entropically (pink) and enthalpically (orange) dominated "hot
spots" act synergistically by stabilizing  -strand b of hEC1 (red).
(B) Closeup view of the interaction interface. S192N and Y369A/S
(ball and stick) stabilize opposite ends of b. G194S+S shortens the
distance to residues Glu-54[hEC1] and Lys-61[hEC1] (ball and
stick) in d and e,
respectively. Stabilization is transmitted through -sheet
bde to the N terminus of b. All structural
figures were prepared by using Pymol.
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