Glycoside Hydrolases, Family GH73 and a Structural Characterization of GH73 Enzyme FlgJ
| dc.contributor.author | Zaloba, Patryk | |
| dc.contributor.examiningcommittee | Kumar, Ayush (Microbiology) Bieringer, Mario (Chemistry) | en_US |
| dc.contributor.supervisor | Mark, Brian (Microbiology) | en_US |
| dc.date.accessioned | 2016-01-14T16:19:51Z | |
| dc.date.available | 2016-01-14T16:19:51Z | |
| dc.date.issued | 2015 | |
| dc.degree.discipline | Microbiology | en_US |
| dc.degree.level | Master of Science (M.Sc.) | en_US |
| dc.description.abstract | 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. | en_US |
| dc.description.note | February 2016 | en_US |
| dc.identifier.uri | http://hdl.handle.net/1993/31067 | |
| dc.language.iso | eng | en_US |
| dc.rights | open access | en_US |
| dc.subject | Crystal Structure | en_US |
| dc.title | Glycoside Hydrolases, Family GH73 and a Structural Characterization of GH73 Enzyme FlgJ | en_US |
| dc.type | master thesis | en_US |