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Figure 4.
Figure 4. The Primary Interface between InlB LRR and Met Ig1
(A) The InlB LRR embraces only the top of Met Ig1 with the
unusual β-wing of the long B-C loop. The LRRs are numbered, and
the strands in Ig1 are labeled. Exposed aromatic side chains at
the concave face of the InlB LRR and the disulfide bond
connecting strands D and E of Met Ig1 are shown as sticks.
(B) Close-up showing InlB Y170^i and Y214^i interacting with
K599^M and K600^M of Met. Y170^i makes hydrogen bonds (dotted
orange lines) to the carbonyl of K599^M and the R602^M side
chain. The side chains of K599^M and K600^M are held in place by
an intra- and intermolecular salt bridge (dotted purple lines),
respectively.
(C) Side chains of residues from β strands
C, F, and G of the Met Ig1 domain form a hydrophobic pocket into
which W124^i from the concave face of the InlB LRR binds.
(D) Electrostatic potential of InlB[321] (left) and Met (right;
Ig2 omitted). In the open-book view, the surfaces involved in
binding are shown for both proteins. The negative charges (red)
on the InlB LRR face positive charges (blue) on Met Ig1.
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