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. 2012 Dec;13(8):831–842. doi: 10.2174/138920312804871210

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© 2012 Bentham Science Publishers

This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.5/), which permits unrestrictive use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. (2) — Structure of ExoS, ExoT, ExoY and ExoU of P. aeruginosa. P. aeruginosa ExoS and ExoT are bifunctional Type III–secreted cytotoxins. Both have an S-domain, CBD, MLD, and C-domain, and GAP and ADPRT activities. ExoS requires Arg146 for the GAP activity, and both Glu379 and Glu381 are required for ADPRT activity. Arg149 is required for the GAP activity of ExoT, and residues Glu383 and Glu385 are crucial for its ADPRT activity. ExoU contains a patatin-like domain that is necessary for phospholipase A2 activity. Residues Ser142 and Asp344 are required for this activity. ExoY is a 378-amino acid adenylyl cyclase. Residues Lys81, Lys88, Asp212 and Asp214 are required for its activity and are thought to be necessary for interactions between ExoY and ATP. S: secretion signal, CBD: chaperone binding domain, MLD: membrane localization domain, GAP: GTPase activating protein, ADPRT: ADP ribosyl transferase; C: cofactor binding site.