Stefano Benini

2009-    Assistant Professor at the Free University of Bolzano

2007-2009         Protein crystallographer in the pharmaceutical company AstraZeneca plc., United Kingdom

2002-2007         Post Doc, York Structural Biology Laboratory, Department of Chemistry, University of York, United Kingdom

2000-2002         Post Doc, International Centre for Genetic Engineering and Biotechnology (ICGEB) Trieste, Italy

1996-2000         PhD student, European Molecular Biology Laboratory (EMBL) Hamburg (Germany)

1992-1996         Msc research assistant, Istituto di Chimica Agraria, Università di Bologna, Bologna, Italy


2000     Ph.D. thesis defence: “Structure and Function Relationships of Urease and Cytochrome c-553 from Bacillus pasteurii“York Structural Biology Laboratory, Department of Chemistry, University of York, United Kingdom

19962000       Study for a doctoral degree in Chemistry (c/o EMBL Hamburg)

1991     Master thesis, in Agricultural Science: “Allevamento in vitro delle larve di Pseudogonia rufifrons Wied. (Dipt. Tachinidae). Prove su diete subnaturali e meridiche“, 108/110. University of Bologna, Bologna Italy

Since my appointment in Bolzano, I devoted myself to the development of the Bioorganic chemistry and Bio-Crystallography laboratory. In few years, my laboratory has characterized and solved the structure of several proteins that are deposited in the PDB. The most important achievement was the structural characterization of the complete biosynthetic pathway of desferrioxamine E, the siderophore of E. amylovora. This pathway includes a pyridoxal dependent lysine decarboxylase (DfoJ), a cadaverine monooxygenase (DfoA) and a desferrioxamine synthetase (DfoC). With the structure solution of the cysteine protease effector AvrRpt2 we shed light onto the induced mechanism of plant resistance to fire blight by Malus x robusta 5. We are the only laboratory using this approach to study the molecular basis of fire blight.

During my PhD, my contribution was pivotal in the proposal of urease reaction mechanism by solving the structure of the enzyme from Sporosarcina pasteurii (previously Bacillus pasteurii) in the native form and in complex with several inhibitors.

Main research areas

Structural and functional characterization of proteins and enzymes from the phyopathogen Erwinia amylovora, the agent of fire blight, and of enzymes with a potential use in biotechnology. Bacterial iron metabolism, carbohydrate-active enzymes, metalloproteins. Other successful areas of interest are: Aspergillus fumigatus siderophore biosynthetic pathway, Malus domestica dihydrochalcones biosynthetic pathway.