FlgJ belongs to Carbohydrate Active enZyme (CAZy) family GH73 and facilitates
passage of the bacterial flagellum through the peptidoglycan (PG) layer by cleaving the
glycosidic bonds within glycan strands of PG. In this thesis I present the structure of
the GH73 enzyme FlgJ from bacterial pathogenSalmonella typhimurium (St FlgJ). The
St FlgJ active site was found to be blocked by the C-terminus of a neighbouring
symmetry mate. To investigate if the C-terminus of FlgJ inhibits enzymatic activity
similarly to the N-terminus of GH73 enzyme Auto, the glycolytic activity of St FlgJ was
measured with and without its C-terminus. The assays revealed St FlgJ activity to be
unaffected by the presence of the C-terminal sequence. Removal of the C-terminus
did, however, allow a crystal structure of the domain to be obtained where a β-hairpin
known to accommodate critical catalytic residues was found capable of opening widely,
which likely aids in substrate capture and turnover. / February 2016
| Identifer | oai:union.ndltd.org:MANITOBA/oai:mspace.lib.umanitoba.ca:1993/31067 |
| Date | 14 January 2016 |
| Creators | Zaloba, Patryk |
| Contributors | Mark, Brian (Microbiology), Kumar, Ayush (Microbiology) Bieringer, Mario (Chemistry) |
| Source Sets | University of Manitoba Canada |
| Detected Language | English |
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