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You searched for id:"oai:scholars.wlu.ca:etd-3230". One record found.

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Wilfrid Laurier University

1. Scott, William. Structural Investigation of BcsC: Insight into Periplasmic Transport During Cellulose Export.

Degree: 2019, Wilfrid Laurier University

A biofilm can be defined by a community of microbes coexisting within a self-produced protective polymeric matrix. Exopolysaccharide (EPS) is a key component in biofilms and a contributor to their virulence and pathogenicity. The cellulose bacterial synthesis complex is one such EPS system that is found in many Enterobacteriaceae,including Escherichia coli and Salmonella spp., and is responsible for the production and secretion of the EPS cellulose. BcsC is the periplasmic protein responsible for the export of the exopolysaccharide cellulose and was the focus of this research. Sequence homology comparisons and structural predictions between BcsC, and the previously characterized alginate export proteins AlgK and AlgE indicate similar roles in facilitating the translocation of EPS across the bacterial cell wall. However, there are discrepancies between the systems, such as the purpose of several additional tetratricopeptide regions (TPRs) contained within BcsC compared to AlgK. To better understand the role that BcsC plays in cellulose export structural characterization of this protein was pursued. Six protein constructs that together cover overlapping portions of BcsCs TPR region were successfully expressed and purified, four of which were further analyzed with SAXS and screened for crystal formation. SAXS data was merged with a pre-existing protein data bank file of BcsCTPR 1-6 to identify similar regions and provided conceptual renderings as to the orientation and size of the protein. Promising crystal hits from BcsCTPR 12-21and BcsCTPR 1-15 were obtained, optimized and sent for X-ray diffraction, with resolution results between 12 and 2.8 Å. A complete dataset for BcsCTPR 1-15 has since been collected and structure solution is ongoing through a combination of molecular replacement and selenomethionine (SeMet) labelling techniques. Preliminary SeMet crystals are promising, but currently appear thinner than native crystals and additional optimization may be required before suitable X-ray diffraction data can be obtained.

Subjects/Keywords: Biochemistry; Structural Biology; Biofilm; Microbiology; Microbial Cellulose; Biochemistry; Microbiology; Molecular Biology; Structural Biology

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Scott, W. (2019). Structural Investigation of BcsC: Insight into Periplasmic Transport During Cellulose Export. (Thesis). Wilfrid Laurier University. Retrieved from https://scholars.wlu.ca/etd/2111

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Scott, William. “Structural Investigation of BcsC: Insight into Periplasmic Transport During Cellulose Export.” 2019. Thesis, Wilfrid Laurier University. Accessed January 23, 2019. https://scholars.wlu.ca/etd/2111.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Scott, William. “Structural Investigation of BcsC: Insight into Periplasmic Transport During Cellulose Export.” 2019. Web. 23 Jan 2019.

Vancouver:

Scott W. Structural Investigation of BcsC: Insight into Periplasmic Transport During Cellulose Export. [Internet] [Thesis]. Wilfrid Laurier University; 2019. [cited 2019 Jan 23]. Available from: https://scholars.wlu.ca/etd/2111.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Scott W. Structural Investigation of BcsC: Insight into Periplasmic Transport During Cellulose Export. [Thesis]. Wilfrid Laurier University; 2019. Available from: https://scholars.wlu.ca/etd/2111

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

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