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Mol Membr Biol. 2010 Apr;27(2-3):104-13. doi: 10.3109/09687680903581267.

Identification of active site residues in the Shigella flexneri glucosyltransferase GtrV.

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  • 1Division of Biomedical Science and Biochemistry, Research School of Biology, College of Medicine, Biology & Environment, Australian National University, Canberra, Australia.

Abstract

The serotype-specific glucosyltransferase, GtrV, is responsible for glucosylation of the O-antigen repeating unit of Shigella flexneri serotype 5a strains. GtrV is an integral inner membrane protein with two essential periplasmic loops: the large Loop 2 and the C-terminal Loop 10. In this study, the full length of the Loop 2 was shown to be necessary for GtrV function. Site-directed mutagenesis within this loop revealed that conserved aromatic and charged amino acids have a critical role in the formation of the active site. Sequential deletions of the C-terminal end indicated that this region may be essential for assembly of the protein in the cytoplasmic membrane. The highly conserved FWAED motif is thought to form the substrate-binding site and was found to be critical in GtrV and GtrX, a serotype-specific glucosyltransferase with homology to GtrV. The data presented constitutes a targeted analysis of the formation of the GtrV active site and highlights the essential role of the large periplasmic Loop 2 in its function.

PMID:
20334579
[PubMed - indexed for MEDLINE]
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