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. Author manuscript; available in PMC: 2007 Feb 28.
Published in final edited form as: Mol Microbiol. 2000 May;36(4):806–816. doi: 10.1046/j.1365-2958.2000.01910.x

Fig. 8.

Fig. 8

Hypothetical structural model for the E.coli Aer protein visualizing the predicted position of residues involved in aerotaxis. The Aer PAS domain (residues 1 to 119) was aligned with the PYP sequence (residues 1 to 125). The alignment was adjusted to minimize energy based on a sudo-Sippl field and submitted to the ProMod II program using the SWISS-PDB viewer. The figure was generated using the MOLSCRIPT program (Kraulis, 1991). Cysteine replacement of the residues shown as stick models produced a null aerotaxis phenotype (red), a loss of FAD binding and a null phenotype (green), inverted responses (yellow) and a CW signaling bias (purple).

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