User:Michael Suits

Michael Suits obtained his BScH in Biochemistry from Queen's University (Canada) and completed his PhD under the supervision of Zongchao Jia at Queen's University. In 2007 he obtained an EMBO Long-term Fellowship to work with Gideon Davies at the York Structural Biology Lab (University of York, York, UK) where his work focused on glycoside hydrolases from families GH26, GH38, GH85, and GH92, and glycosyltransferase family GT78. In 2007 he joined Alisdair Boraston at the University of Victoria (Canada) and was awarded a Michael Smith Foundation for Health Research Fellowship in 2008 to continue work on microbial CAZymes. He is now an Assistant Professor in the Department of Chemistry at Wilfrid Laurier University (Canada) where his work uses X-ray crystallography and various biophysical tools to characterize carbohydrate metabolizing factors.

Michael and colleagues have characterized the X-ray crystal structures of:

• CBM32-4, CBM32-5, CBM32-6 Clostridium perfringens appended to exo-α-D-N-acetylglucosaminidase (GH89) [1].
• GH26 Cellvibrio japonicus GH26 mannanase [2].
• GH38 Streptococcus pyogenes α-mannosidase [3].
• GH85 Arthrobacter protophormiae endo-beta-D-N-acetylglucosaminidases (EndoA) [4].
• GH92 Bacteroides thetaiotaomicron α-mannosidase [5].
• GH-Non-Classified Streptococcus pyogenes plasmin and fibronectin binding protein A (PfbA) [6].
• GT78 Rhodothermus marinus mannosylglycerate synthase [7].

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1. Ficko-Blean E, Stuart CP, Suits MD, Cid M, Tessier M, Woods RJ, and Boraston AB. (2012). Carbohydrate recognition by an architecturally complex α-N-acetylglucosaminidase from Clostridium perfringens. PLoS One. 2012;7(3):e33524. DOI:10.1371/journal.pone.0033524 |
2. Cartmell A, Topakas E, Ducros VM, Suits MD, Davies GJ, and Gilbert HJ. (2008). The Cellvibrio japonicus mannanase 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. 2008;283(49):34403-13. DOI:10.1074/jbc.M804053200 |
3. Suits MD, Zhu Y, Taylor EJ, Walton J, Zechel DL, Gilbert HJ, and Davies GJ. (2010). Structure and kinetic investigation of Streptococcus pyogenes family GH38 alpha-mannosidase. PLoS One. 2010;5(2):e9006. DOI:10.1371/journal.pone.0009006 |
4. Ling Z, Suits MD, Bingham RJ, Bruce NC, Davies GJ, Fairbanks AJ, Moir JW, and Taylor EJ. (2009). The X-ray crystal structure of an Arthrobacter protophormiae endo-beta-N-acetylglucosaminidase reveals a (beta/alpha)(8) catalytic domain, two ancillary domains and active site residues key for transglycosylation activity. J Mol Biol. 2009;389(1):1-9. DOI:10.1016/j.jmb.2009.03.050 |
5. Zhu Y, Suits MD, Thompson AJ, Chavan S, Dinev Z, Dumon C, Smith N, Moremen KW, Xiang Y, Siriwardena A, Williams SJ, Gilbert HJ, and Davies GJ. (2010). Mechanistic insights into a Ca2+-dependent family of alpha-mannosidases in a human gut symbiont. Nat Chem Biol. 2010;6(2):125-32. DOI:10.1038/nchembio.278 |
6. Suits MD and Boraston AB. (2013). Structure of the Streptococcus pneumoniae surface protein and adhesin PfbA. PLoS One. 2013;8(7):e67190. DOI:10.1371/journal.pone.0067190 |
7. Nielsen MM, Suits MD, Yang M, Barry CS, Martinez-Fleites C, Tailford LE, Flint JE, Dumon C, Davis BG, Gilbert HJ, and Davies GJ. (2011). Substrate and metal ion promiscuity in mannosylglycerate synthase. J Biol Chem. 2011;286(17):15155-64. DOI:10.1074/jbc.M110.199844 |