Figure 2

Structural overlay of YopM-InlB with wild type InlB ₃₂₁ and YopM. (A) YopM-InlB is colored orange and green as in Figure 1. Residues 34–87 from YopM (dark grey) and residues 93–321 from wild type InlB (light grey) are structurally aligned to highlight overall similarity and local differences. (B) YopM-InlB (colored as in Figure 1 and Figure 2A) was structurally aligned with InlB (grey). LRR1, which carries different sequences in the two proteins, shows the largest structural deviations. However, residues on the concave face of LRR2 and LRR3 are also shifted. (C) Overlay of YopM-InlB (colored as in Figure 1 and Figure 2A,B) onto InlB₃₂₁ (grey) in the complex with MET (brown) (PDB ID 2uzx). Due to the shift in LRR1 residues Glu75 and Asn79 from YopM-InlB cannot form the hydrogen bonds to MET that are formed by the equivalent residues from wild type InlB (Gln80 and Asn84, respectively).