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Biochem Biophys Res Commun. 2008 Oct 31;375(4):581-5. doi: 10.1016/j.bbrc.2008.08.069. Epub 2008 Aug 26.

Topology and identification of critical residues of the O-acetyltransferase of serotype-converting bacteriophage, SF6, of Shigella flexneri.

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  • 1School of Biochemistry and Molecular Biology, Faculty of Science, The Australian National University, ACT 0200, Australia.


The modification of the LPS O-antigen, seen in the diverse serotypes of Shigella flexneri is brought about by the glucosyltransferases (Gtr) and the O-acetyltransferase (Oac). In this study, we establish the membrane topology of Oac using the dual reporter PhoA-LacZalpha. We have determined that Oac is an integral membrane protein with 10 transmembrane regions. The hydrophilic N- and C-termini are oriented in the cytoplasm. Functionally important cytoplasmic and periplasmic loops have also been identified. Furthermore, cytoplasmic residues R73 and R75R76 were found to be critical to Oac function.

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