Supplementary Figure 1: The sequence and secondary structure of YopO and its interaction with actin.

Sequence/structural analysis of YopO of Yersinia enterocolitica (89-729) (accession NP_783721) aligned against YpkA of Yersinia pestis (accession NP_395206) and Yersinia pseudotuberculosis (accession YP_068414). The secondary structure of the kinase and GDI domains are indicated in blue and red above the sequence alignment, respectively. Disordered regions are represented by disconnected lines. The putative phosphorylation sites Ser90 and Ser95 are marked with black circles. The surface entropy reduction mutations are indicated by black asterisks. Residues that constitute the αC helix, the catalytic loop and the activation segment are shown in magenta, red and green, respectively. The catalytic residue Asp267 is marked with a red circle and residues involved in interaction with actin and Rac1 are indicated with cyan and yellow squares, respectively. The alignment was performed using Clustal Omega and drawn with ESPript.