Associate Professor and Research Group leader at the Department of Chemistry, University of Copenhagen.
Short biographical sketch
Italian, born in Palermo 1971. Educated in Biochemistry at the University of Bath, during which had two inspiring introductions to the world of research in the groups of Roy Jones at the Babraham station and Angelika Noegel at the Max-Planck Institute for Biochemistry in Munich. Obtained a PhD in Crystallography from Birkbeck College, London, in 1997. In fact my PhD research was carried out at the Institute of Food Research in Reading, under the supervision of Richard Pickersgill. The project revolved around structure determination of xylanases and cellulases, and I was fortunate by being involved in the establishment of the 4/7 superfamily , then to become Clan GH-A .
I was then post-doctoral fellow in the group of Sine Larsen, at the Department of Chemistry, University of Copenhagen, first funded by a personal EMBO fellowship and later by other grants, until 2003, when I obtained a permanent position as Associate Professor in the same Department. In 2005 I became Research Group leader of the Biophysical Chemistry Group, still in the same Department. In 2013 the Biophysical Chemistry Group became part of the Bioinorganic and Biophysical Chemistry Section. Studies on the structure and function of carbohydrate active enzymes remains one of my major areas of research here in Copenhagen. My other main branch of research is on transcription factors.
I have either determined or contributed to structure determination, and structure/function and mechanistic elucidation in of a number of CAZY in GH5, GH9, GH10, GH13, GH26, GH31, GH36, GH53, PL4 and AA9. Some of my articles on CAZYs are in the reference list below [3, 4, 5, 6, 7, 8, 9].
- Jenkins J, Lo Leggio L, Harris G, and Pickersgill R. Beta-glucosidase, beta-galactosidase, family A cellulases, family F xylanases and two barley glycanases form a superfamily of enzymes with 8-fold beta/alpha architecture and with two conserved glutamates near the carboxy-terminal ends of beta-strands four and seven. FEBS Lett. 1995 Apr 10;362(3):281-5.
- Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, and Davies G. Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases. Proc Natl Acad Sci U S A. 1996 May 28;93(11):5674.
- Harris GW, Jenkins JA, Connerton I, Cummings N, Lo Leggio L, Scott M, Hazlewood GP, Laurie JI, Gilbert HJ, and Pickersgill RW. Structure of the catalytic core of the family F xylanase from Pseudomonas fluorescens and identification of the xylopentaose-binding sites. Structure. 1994 Nov 15;2(11):1107-16.
- Le Nours J, Anderson L, Stoll D, Stålbrand H, and Lo Leggio L. The structure and characterization of a modular endo-beta-1,4-mannanase from Cellulomonas fimi. Biochemistry. 2005 Sep 27;44(38):12700-8. DOI:10.1021/bi050779v |
- Ernst HA, Lo Leggio L, Willemoës M, Leonard G, Blum P, and Larsen S. Structure of the Sulfolobus solfataricus alpha-glucosidase: implications for domain conservation and substrate recognition in GH31. J Mol Biol. 2006 May 12;358(4):1106-24. DOI:10.1016/j.jmb.2006.02.056 |
- Ryttersgaard C, Lo Leggio L, Coutinho PM, Henrissat B, and Larsen S. Aspergillus aculeatus beta-1,4-galactanase: substrate recognition and relations to other glycoside hydrolases in clan GH-A. Biochemistry. 2002 Dec 24;41(51):15135-43.
- Le Nours J, Ryttersgaard C, Lo Leggio L, Østergaard PR, Borchert TV, Christensen LL, and Larsen S. Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. Protein Sci. 2003 Jun;12(6):1195-204. DOI:10.1110/ps.0300103 |
- Ryttersgaard C, Le Nours J, Lo Leggio L, Jørgensen CT, Christensen LL, Bjørnvad M, and Larsen S. The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. J Mol Biol. 2004 Jul 30;341(1):107-17. DOI:10.1016/j.jmb.2004.05.017 |
- Le Nours J, De Maria L, Welner D, Jørgensen CT, Christensen LL, Borchert TV, Larsen S, and Lo Leggio L. Investigating the binding of beta-1,4-galactan to Bacillus licheniformis beta-1,4-galactanase by crystallography and computational modeling. Proteins. 2009 Jun;75(4):977-89. DOI:10.1002/prot.22310 |