User:Lynne Howell

Lynne Howell obtained an undergraduate degree in Biophysics from the University of Leeds in 1983 and a Ph.D. in Crystallography from the University of London under the guidance of Prof. Dame Jane Goodfellow. She spent three years as a postdoctoral fellow with Professor Gregory Petsko at the Massachusetts Institute of Technology before moving to Paris to study with Dr. Roberto Poljak and Dr. André Menez at the Institut Pasteur. After a year as a staff scientist in Paris, Dr. Howell joined The Hospital of Sick Children in Toronto in late 1991 and was cross appointed to the University of Toronto shortly thereafter. She’s a recipient of a Canada Research Chair in Structural Biology and her research is focused on microbial biofilm formation, specifically understanding at the molecular level the exopolysaccharide biosynthetic systems of various bacteria and fungi (more information can be found on the laboratory webpage). This work has involved collaborations with Prof. Anthony Clarke, Prof. Mark Nitz, Prof. Jeroen Codée, Prof. John Klassen, Prof. Don Sheppard and Prof. Joel Weadge, among others.

Her lab has determined the crystal structures of multiple carbohydrate active enzymes including (but not limited to):

• GH39 Pseudomonas aeruginosa PslG, PSL polysaccharide hydrolase [1]
• GH47 Penicillium citrinum α-1,2-mannosidase [2]
• GH114 Aspergillus fumigatus Ega3, an α-1,4-galactosaminidase [3]
• GH135 Aspergillus clavatus Sph3, an α-1,4-N-acetylgalactosaminidase  [4]
• GH153 Bordetella bronchiseptica PgaB (C-terminal domain), a poly-β-1,6-D-glucosamine hydrolase [5]
• GH166 Pseudomonas aeruginosa PelA (N-terminal domain), α-1,4-N-acetylgalactosaminidase [6]
• CE4 Ammonifex degensii IcaB, a poly-β-1,6-N-acetyl-D-glucosamine deacetylase [7] 
• CE4 Bordetella bronchiseptica PgaB (N-terminal domain), a poly-β-1,6-N-acetyl-D-glucosamine deacetylase [8]
• CE4/GH153 Escherichia coli PgaB, a poly-β-1,6-D-glucosamine deacetylase and hydrolase [9]
• CE18 and CBM87 Aspergillus fumigatus Agd3, an α-1,4-N-acetylgalactosaminidase deacetylase [10] 
• PL5 Pseudomonas aeruginosa AlgL, (no associated paper)
• PL7 Klebsiella pneumoniae Alginate lyase, (no associated paper)
• GT15 Saccharomyces cerevisiae ⍺-1,2-monnosyltransferase complex Kre2p/Mnt1p [11]
• Pseudomonas syringae AlgG, β-D-mannuronate (alginate) C5-epimerase [12]
• Pseudomonas putida AlgJ, involved in alginate O-acetylation [13]
• Pseudomonas aeruginosa AlgX, alginate O-acetylase [14]
• Pseudomonas protegens PelX, a C-4 epimerase that interconverts UDP-GalNAc and UDP-GlcNAc [15]
• Bacillus cereus PatB1, peptidoglycan O-acetylase [16]
• Streptococcus pneumoniae OatA, peptidoglycan O-acetylase [17]
• Staphylococcus aureus OatA, peptidoglycan O-acetylase [18]

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12. Wolfram F, Kitova EN, Robinson H, Walvoort MT, Codée JD, Klassen JS, and Howell PL. (2014). Catalytic mechanism and mode of action of the periplasmic alginate epimerase AlgG. J Biol Chem. 2014;289(9):6006-19. DOI:10.1074/jbc.M113.533158 |