Assistant Professor, Chemistry and Biochemistry
Contact InformationEmail: email@example.com
Phone: 1.519.884.0710 ext.4961 | lab ext.2133
Office Location: Science Building N2065
2013 marked the 100th anniversary of Bragg's Law (2dsin?=n?) ; a key concept that allows crystallographers to relate diffraction patterns back to the atomic properties within a crystal. For those interesting in finding out why this centenary was significant, please refer to the following animated video produced by the Royal Institution: Celebrating Crystallography: An Animated Adventure.
Beyond the universally recognized role for carbohydrates as nutrient sources, complex carbohydrates in the form of polysaccharides, proteoglycans and glycolipids may be considered to be "the language of the cell" in that they mediate many integral biological events. Because of this central importance, research in the Suits Lab utilizes X-ray crystallography and supportive biophysical characterization methods to characterize the interaction between proteins and carbohydrates. Our work focuses on long, linear carbohydrates such as chondroitin, heparan, hyaluronan, alginate and pectin, and addresses the how and why of the microbial factors recognize and process these carbohydrates.
Dr. Suits is an Assistant Professor in the Department of Chemistry & Biochemistry at Wilfrid Laurier University. He received his PhD in Biochemistry from Queen's University where his thesis work with Prof. Zongchao Jia focused on heme processing and a lipopolysaccharide transport protein, LptA. He was a European Molecular Biology Organization Fellow at The York Structural Biology Laboratory (YSBL) at the University of York, UK with Prof. Gideon Davies where his work addressed the structure-function relationship of microbial carbohydrate active enzymes (CAZymes). CAZymes describe families of structurally-related enzymes that degrade, modify, or create glycosidic bonds and the frequently associated carbohydrate-binding modules (please see CAZy and CAZypedia for more details). Dr. Suits continued this research focus on microbial CAZymes at the University of Victoria with Dr. Alisdair Boraston and included a collaboration involving the structural characterization of receptor-antibody complexes with Dr. Martin Boulanger and Zymeworks Inc. (Vancouver, BC).
Publications † Denotes co-first authorship
16. Cuskin, F., Lowe, E.C., Temple, M.J., Zhu, Y., Cameron, E.A., Pudlo, N.A., Porter, N.T., Urs, K., Thompson, A.J., Cartmell, A., Rogowski, A., Hamilton, B.S., Chen, R., Tolbert, T.J., Piens, K., Bracke, D., Vervecken, W., Hakki, Z., Speciale, G., Mun?z-Mun?z, J.L., Day, A., Peña, M.J., McLean, R., Suits, M.D., Boraston, A.B., Atherly, T., Ziemer, C.J., Williams, S.J., Davies, G.J., Abbott, D.W., Martens, E.C., Gilbert, H.J. (2014). Human gut Bacteroidetes can utilize yeast mannan through a selfish mechanism. Nature 517(7533):165-9.
15. Suits, M.D.†, Pluvinage, B., Law, A., Liu, Y., Palma, A.S., Chai, W., Feizi, T., Boraston, A.B. (2014). Conformational Analysis of the Streptococcus pneumoniae Hyaluronate Lyase and Characterization of Its Hyaluronan-specific Carbohydrate-binding Module. JBC 289(39):27264-77.
14. Higgins, M.A., Suits, M.D., Marsters, C., Boraston, A.B. (2014). Structural and Functional Analysis of Fucose-Processing Enzymes from Streptococcus pneumoniae. J Mol Biol. 426(7):1469-82.
13. Von Kreudenstein T.S., Escobar E., Lario P.I., D'Angelo I., Brault K., Kelly J., Durocher Y., Baardsnes J., Woods J.R., Xie M.H., Girod P.A., Suits, M.D., Boulanger M.J., Poon D., Ng G.Y., Dixit S.B. (2013). Improving biophysical properties of a bispecific antibody scaffold to aid developability: Quality by molecular design. MAbs 5(5):646-54.
12. Suits, M.D., Boraston, A.B. (2013). Structure of the Streptococcus pneumoniae surface protein and adhesin PfbA. PLOS-One 8(7):e67190.
11. Ficko-Blean E., Stuart, C.P., Suits, M.D., Cid, M., Tessier, M., Woodsm R.J., Boraston, A.B. (2012). Carbohydrate Recognition by an Architecturally Complex ?-N-Acetylglucosaminidase from Clostridium perfringens. PLOS-One 7(3):e33524.
10. Nielsen, M.M.†, Suits, M.D.†, Yang, M., Barry, C.S., Martinez-Fleites, C., Tailford, L.E., Flint, J.E., Davis, B.G., Davies, G.J., Gilbert, H.J. (2011). Substrate and metal-ion promiscuity in mannosylglycerate synthase. JBC 286(17):15155-64.
9. Suits, M.D., Zhu, Y., Taylor, E.J., Walton, J., Zechel, D.L., Gilbert, H.J., Davies, G.J. (2010). Structure and kinetic investigation of Streptococcus pyogenes family GH38 a-mannosidase. PLOS-One 5(2):e9006.
8. Zhu, Y., Suits, M.D.†, Thompson, A.J., Chavan, S., Dinev, Z., Dumon, C., Smith, N., Moremen, K.W., Xiang, Y., Siriwardena, A., Williams, S.J., Gilbert, H.J., Davies, G.J. (2010). Mechanistic insights into a Ca2+-dependent family of ?-mannosidases in a human gut symbiont. Nat Chem Biol. 6(2):125-32.
7. Ling, Z., Suits, M.D.†, Bingham, R.J., Bruce, N.C., Davies, G.J., Fairbanks, A.J., Moir, J.W., Taylor, E.J. (2009). The X-ray Crystal Structure of an Arthrobacter protophormiae Endo-?-N-Acetylglucosaminidase Reveals a (?/?)8 Catalytic Domain, Two Ancillary Domains and Active Site Residues Key for Transglycosylation Activity. J Mol Biol. 389(1):1-9.
6. Suits, M.D., Lang, J., Pal, G.P., Couture, M., Jia, Z. (2009). Structure and heme binding properties of Escherichia coli O157:H7 ChuX. Protein Sci. 18(4):825-38.
5. Cartmell, A., Topakas, E., Ducros, V.M-A., Suits, M.D., Davies, G.J., Gilbert, H.J. (2008). The Cellvibrio Japonicus Mannase CJMAN26C Displays a Unique Exo-mode of Action That is Conferred by Subtle Changes to the Distal Region of the Active Site. J Biol Chem. 283(49):34403-13.
4. Suits, M.D., Sperandeo, P., Dehò, G., Polissi, A., Jia, Z. (2008). Novel structure of the conserved Gram-negative lipopolysaccharide transport protein LptA and mutagenesis analysis. J Mol Biol. 380(3):476-88.
3. Adams, M.A., Suits, M.D., Zheng, J., Jia, Z. (2007). Piecing together the Structure-Function Puzzle: Experiences in structure-based functional annotation of hypothetical proteins. Proteomics (16):2920-32. Review
2. Suits, M.D., Jaffer, N., Jia, Z. (2006). Structure of the Escherichia coli O157:H7 heme oxygenase ChuS in complex with heme and enzymatic inactivation by mutation of the heme coordinating residue His 193. JBC 281(48):36776-82.
1. Suits, M.D., Pal, G.P., Nakatsu. K., Matte, A., Cygler, M., Jia, Z. (2005). Identification of an Escherichia coli O157:H7 heme oxygenase with tandem functional repeats. Proc Natl Acad Sci 102(47):16955-60.